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1H, 13C and 15N assignment of self-complemented MrkA protein antigen from Klebsiella pneumoniae 肺炎克雷伯氏菌自补体 MrkA 蛋白抗原的 1H、13C 和 15N 赋值。
IF 0.8 4区 生物学 Q4 BIOPHYSICS Pub Date : 2024-07-17 DOI: 10.1007/s12104-024-10185-3
Valentina Monaci, Gianmarco Gasperini, Lucia Banci, Francesca Micoli, Francesca Cantini

Klebsiella pneumoniae (Kp) poses an escalating threat to public health, particularly given its association with nosocomial infections and its emergence as a leading cause of neonatal sepsis, particularly in low- and middle-income countries (LMICs). Host cell adherence and biofilm formation of Kp is mediated by type 1 and type 3 fimbriae whose major fimbrial subunits are encoded by the fimA and mrkA genes, respectively. In this study, we focus on MrkA subunit, which is a 20 KDa protein whose 3D molecular structure remains elusive. We applied solution NMR to characterize a recombinant version of MrkA in which the donor strand segment situated at the protein’s N-terminus is relocated to the C-terminus, preceded by a hexaglycine linker. This construct yields a self-complemented variant of MrkA. Remarkably, the self-complemented MrkA monomer loses its capacity to interact with other monomers and to extend into fimbriae structures. Here, we report the nearly complete assignment of the 13C,15N labelled self-complemented MrkA monomer. Furthermore, an examination of its internal mobility unveiled that relaxation parameters are predominantly uniform across the polypeptide sequence, except for the glycine-rich region within loop 176–181. These data pave the way to a comprehensive structural elucidation of the MrkA monomer and to structurally map the molecular interaction regions between MrkA and antigen-induced antibodies.

肺炎克雷伯氏菌(Kp)对公共卫生的威胁日益严重,特别是考虑到它与医院内感染的关系,以及它已成为新生儿败血症的主要病因,尤其是在中低收入国家(LMICs)。Kp 的宿主细胞粘附和生物膜形成是由 1 型和 3 型缘膜介导的,其主要缘膜亚基分别由 fimA 和 mrkA 基因编码。在本研究中,我们重点研究了MrkA亚基,它是一种20 KDa的蛋白质,其三维分子结构仍然难以捉摸。我们利用溶液核磁共振分析了一种重组版本的 MrkA,其中位于蛋白质 N 端的供体链段被移至 C 端,之前是一个六甘氨酸连接体。这种构建物产生了一种自补体的 MrkA 变体。值得注意的是,自补的 MrkA 单体失去了与其他单体相互作用的能力,也无法延伸到流苏结构中。在这里,我们报告了 13C、15N 标记的自补体 MrkA 单体的近乎完整的分配。此外,对其内部迁移率的研究发现,除了环 176-181 中富含甘氨酸的区域外,整个多肽序列的弛豫参数基本一致。这些数据为全面阐明MrkA单体的结构以及绘制MrkA与抗原诱导抗体之间分子相互作用区域的结构图铺平了道路。
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引用次数: 0
Solid-state NMR assignment of α-synuclein polymorph prepared from helical intermediate 由螺旋中间体制备的α-突触核蛋白多晶体的固态核磁共振分配。
IF 0.8 4区 生物学 Q4 BIOPHYSICS Pub Date : 2024-07-04 DOI: 10.1007/s12104-024-10188-0
Sahil Ahlawat, Surabhi Mehra, Chandrakala M. Gowda, Samir K Maji, Vipin Agarwal

Synucleinopathies are neurodegenerative diseases characterized by the accumulation of α-synuclein protein aggregates in the neurons and glial cells. Both ex vivo and in vitro α-synuclein fibrils tend to show polymorphism. Polymorphism results in structure variations among fibrils originating from a single polypeptide/protein. The polymorphs usually have different biophysical, biochemical and pathogenic properties. The various pathologies of a single disease might be associated with distinct polymorphs. Similarly, in the case of different synucleinopathies, each condition might be associated with a different polymorph. Fibril formation is a nucleation-dependent process involving the formation of transient and heterogeneous intermediates from monomers. Polymorphs are believed to arise from heterogeneous oligomer populations because of distinct selection mechanisms in different conditions. To test this hypothesis, we isolated and incubated different intermediates during in vitro fibrillization of α-synuclein to form different polymorphs. Here, we report 13C and 15N chemical shifts and the secondary structure of fibrils prepared from the helical intermediate using solid-state nuclear magnetic spectroscopy.

突触核蛋白病是一种神经退行性疾病,其特征是α-突触核蛋白蛋白聚集在神经元和神经胶质细胞中。体内和体外α-突触核蛋白纤维都倾向于表现出多态性。多态性导致源自单个多肽/蛋白质的纤维结构发生变化。多态性通常具有不同的生物物理、生物化学和致病特性。一种疾病的各种病理现象可能与不同的多态性有关。同样,在不同的突触核蛋白病中,每种病症都可能与不同的多态性有关。纤维的形成是一个成核依赖过程,涉及从单体形成瞬时和异质的中间体。由于不同条件下的选择机制不同,多态性被认为是由异质的低聚物群体产生的。为了验证这一假设,我们分离并培养了α-突触核蛋白体外纤维化过程中的不同中间产物,以形成不同的多态性。在此,我们利用固态核磁共振谱报告了由螺旋中间体制备的纤维的 13C 和 15N 化学位移和二级结构。
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引用次数: 0
Solid-state NMR backbone chemical shift assignments of α-synuclein amyloid fibrils at fast MAS regime 快速 MAS 机制下 α-突触核蛋白淀粉样纤维的固态 NMR 主干化学位移分配。
IF 0.8 4区 生物学 Q4 BIOPHYSICS Pub Date : 2024-06-29 DOI: 10.1007/s12104-024-10186-2
Zigmantas Toleikis, Piotr Paluch, Ewelina Kuc, Jana Petkus, Darius Sulskis, Mai-Liis Org-Tago, Ago Samoson, Vytautas Smirnovas, Jan Stanek, Alons Lends

The α-synuclein (α-syn) amyloid fibrils are involved in various neurogenerative diseases. Solid-state NMR (ssNMR) has been showed as a powerful tool to study α-syn aggregates. Here, we report the 1H, 13C and 15N back-bone chemical shifts of a new α-syn polymorph obtained using proton-detected ssNMR spectroscopy under fast (95 kHz) magic-angle spinning conditions. The manual chemical shift assignments were cross-validated using FLYA algorithm. The secondary structural elements of α-syn fibrils were calculated using 13C chemical shift differences and TALOS software.

α-突触核蛋白(α-syn)淀粉样纤维与多种神经退行性疾病有关。固态核磁共振(ssNMR)已被证明是研究α-syn聚集体的有力工具。在此,我们报告了在快速(95 kHz)魔角旋光条件下使用质子检测的 ssNMR 光谱获得的一种新的α-syn 多晶体的 1H、13C 和 15N 骨背化学位移。使用 FLYA 算法对手动化学位移分配进行了交叉验证。利用 13C 化学位移差异和 TALOS 软件计算了 α-syn 纤维的二级结构元素。
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引用次数: 0
Backbone and methyl side-chain resonance assignments of the Fab fragment of adalimumab 阿达木单抗 Fab 片段的骨架和甲基侧链共振分配。
IF 0.8 4区 生物学 Q4 BIOPHYSICS Pub Date : 2024-06-26 DOI: 10.1007/s12104-024-10187-1
Muzaddid Sarker, Yves Aubin

Adalimumab is a therapeutic monoclonal antibody developed to target human TNF an important mediator of immune-mediated inflammatory diseases such as rheumatoid arthritis, amongst others. The 48 kDa Fab fragment of adalimumab was produced in Escherichia coli using a single chain approach to allow complete isotopic incorporation of deuterium, carbon-13 and nitrogen-15 along with the protonated isoleucine-d, valine and leucine methyl groups. Here we report the near complete resonance assignment of the polypeptide backbone and the methyl groups of isoleucine, leucine and valine residues.

阿达木单抗是一种治疗性单克隆抗体,针对人类 TNF 而开发,TNF 是类风湿性关节炎等免疫介导炎症性疾病的重要介质。阿达木单抗的 48 kDa Fab 片段是在大肠杆菌中使用单链方法生产的,这种方法可以将氘、碳-13 和氮-15 以及质子化的异亮氨酸-d、缬氨酸和亮氨酸甲基完全同位素化。在此,我们报告了多肽骨架以及异亮氨酸、亮氨酸和缬氨酸残基甲基的近乎完整的共振分配。
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引用次数: 0
Assignment of the Lassa virus transmembrane domain in the prefusion and postfusion states in detergent micelles 拉沙病毒跨膜结构域在洗涤剂胶束中的融合前和融合后状态的分配。
IF 0.8 4区 生物学 Q4 BIOPHYSICS Pub Date : 2024-06-25 DOI: 10.1007/s12104-024-10184-4
Patrick M. Keating, Jinwoo Lee

Lassa virus (LASV) is the most prevalent member of the arenavirus family and the causative agent of Lassa fever, a viral hemorrhagic fever. Although there are annual outbreaks in West Africa, and recently isolated cases worldwide, there are no current therapeutics or vaccines. As such, LASV poses a significant global public health threat. One of the key steps in LASV infection is delivering its genetic material by fusing its viral membrane with the host cell membrane. This process is facilitated by significant conformational changes within glycoprotein 2 (GP2), yielding distinct prefusion and postfusion structural states. However, structural information is missing to understand the changes that occur in the transmembrane domain (TM) during the fusion process. Previously, we showed that the TM undergoes pH-dependent structural changes that result in a helical extension. Here, we provide the 1H, 15N, and 13C assignment of the LASV TM backbone in the prefusion and postfusion states. We also provide the 1H, 15N, and 13C assignment of two mutants, G429P and D432P, which prevent this helical extension. These results will help understand the role the TM plays in membrane fusion and can lead to the design of therapeutics against LASV infection.

拉沙病毒(LASV)是禽流感病毒家族中最流行的成员,也是病毒性出血热--拉沙热的病原体。虽然每年都会在西非爆发,最近在全球范围内也出现了个别病例,但目前还没有治疗方法或疫苗。因此,LASV 对全球公共卫生构成了重大威胁。LASV 感染的关键步骤之一是通过将病毒膜与宿主细胞膜融合来传递其遗传物质。糖蛋白 2(GP2)的构象发生了重大变化,产生了不同的融合前和融合后结构状态,从而促进了这一过程。然而,要了解融合过程中跨膜结构域(TM)发生的变化,还缺少结构信息。此前,我们发现跨膜结构域(TM)发生了 pH 依赖性结构变化,导致螺旋延伸。在此,我们提供了 LASV TM 主干在融合前和融合后状态下的 1H、15N 和 13C 赋值。我们还提供了两个突变体(G429P 和 D432P)的 1H、15N 和 13C 赋值,这两个突变体阻止了这种螺旋延伸。这些结果将有助于了解 TM 在膜融合中的作用,并有助于设计治疗 LASV 感染的药物。
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引用次数: 0
NMR resonance assignment of the cell death execution domain BELL2 from multicellular bacterial signalosomes 多细胞细菌信号体中细胞死亡执行结构域 BELL2 的核磁共振分配。
IF 0.8 4区 生物学 Q4 BIOPHYSICS Pub Date : 2024-06-22 DOI: 10.1007/s12104-024-10183-5
Loic Delcourte, Corinne Sanchez, Estelle Morvan, Mélanie Berbon, Axelle Grélard, Claire Saragaglia, Thierry Dakhli, Stéphane Thore, Benjamin Bardiaux, Birgit Habenstein, Brice Kauffmann, Sven J. Saupe, Antoine Loquet

Signalosomes are high-order protein machineries involved in complex mechanisms controlling regulated immune defense and cell death execution. The immune response is initiated by the recognition of exogeneous or endogenous signals, triggering the signalosome assembly process. The final step of signalosome fate often involves membrane-targeting and activation of pore-forming execution domains, leading to membrane disruption and ultimately cell death. Such cell death-inducing domains have been thoroughly characterized in plants, mammals and fungi, notably for the fungal cell death execution protein domain HeLo. However, little is known on the mechanisms of signalosome-based immune response in bacteria, and the conformation of cell death executors in bacterial signalosomes is still poorly characterized. We recently uncovered the existence of NLR signalosomes in various multicellular bacteria and used genome mining approaches to identify putative cell death executors in Streptomyces olivochromogenes. These proteins contain a C-terminal amyloid domain involved in signal transmission and a N-terminal domain, termed BELL for Bacteria analogous to fungal HeLL (HeLo-like), presumably responsible for membrane-targeting, pore-forming and cell death execution. In the present study, we report the high yield expression of S. olivochromogenes BELL2 and its characterization by solution NMR spectroscopy. BELL is folded in solution and we report backbone and sidechain assignments. We identified five α-helical secondary structure elements and a folded core much smaller than its fungal homolog HeLo. This study constitutes the first step toward the NMR investigation of the full-length protein assembly and its membrane targeting.

信号体是一种高阶蛋白质机制,参与控制调节免疫防御和细胞死亡执行的复杂机制。免疫反应是通过识别外源或内源信号,触发信号体组装过程而启动的。信号体命运的最后一步往往涉及膜靶向和激活孔形成执行域,导致膜破坏,最终导致细胞死亡。在植物、哺乳动物和真菌中,这种诱导细胞死亡的结构域已被彻底表征,特别是真菌细胞死亡执行蛋白结构域 HeLo。然而,人们对细菌中基于信号体的免疫反应机制知之甚少,而且对细菌信号体中细胞死亡执行蛋白的构象仍然知之甚少。我们最近发现了多种多细胞细菌中存在的 NLR 信号体,并利用基因组挖掘方法鉴定了橄榄色链霉菌中的推定细胞死亡执行体。这些蛋白质包含一个参与信号传递的 C 端淀粉样结构域和一个 N 端结构域(BELL,表示细菌类似于真菌的 HeLL(HeLo-like)),可能负责膜靶向、孔形成和细胞死亡执行。在本研究中,我们报告了 S. olivochromogenes BELL2 的高产率表达及其溶液核磁共振光谱特性。BELL 在溶液中折叠,我们报告了骨架和侧链的分配。我们发现了五个α螺旋二级结构元素和一个折叠核心,其体积远小于其真菌同源物 HeLo。这项研究为全长蛋白质的组装及其膜靶向的核磁共振研究迈出了第一步。
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引用次数: 0
Backbone NMR resonance assignments for the VP1u N-terminal receptor-binding domain of the human parvovirus pathogen B19 人类副病毒病原体 B19 的 VP1u N 端受体结合域的骨架核磁共振共振分配。
IF 0.8 4区 生物学 Q4 BIOPHYSICS Pub Date : 2024-06-21 DOI: 10.1007/s12104-024-10181-7
Maria Luiza Caldas Nogueira, Renuk Lakshmanan, Gwladys Rivière, Mario Mietzsch, Antonette Bennett, Robert McKenna, Joanna R. Long

Parvovirus B19 (B19V) is a human pathogen that is the causative agent of several diseases in infants and adults. Due to a lack of antivirals against this virus, treatment options are limited. The minor capsid protein of B19V has a unique N terminus, named VP1u, which is essential for infection. The VP1u encodes a receptor binding domain (RBD), necessary for host cell entry, and a phospholipase A2 (PLA2) domain, crucial for endosomal escape during cellular trafficking. Both domains are indispensable for infection, making the RBD a plausible drug target for inhibitors against B19V, as it is located on the exterior surface of the virus. To date, no experimental structural information has been available for the VP1u component for any Parvovirus. Here we report the backbone NMR resonance assignments for the RBD of B19V and demonstrate it forms a stable structure. The backbone chemical shifts are in good agreement with a structure predicted by AlphaFold, validating that the RBD contains three helices connected by tight turns. This RBD construct can now be used for further NMR studies, including assignment of full-length VP1u, determination of protein-protein interaction interfaces, and development of B19 antivirals specific to the RBD domain.

Parvovirus B19(B19V)是一种人类病原体,是婴儿和成人多种疾病的病原体。由于缺乏针对这种病毒的抗病毒药物,治疗方案十分有限。B19V 的小囊膜蛋白有一个独特的 N 末端,名为 VP1u,它对感染至关重要。VP1u 编码一个受体结合结构域(RBD)和一个磷脂酶 A2(PLA2)结构域,前者是宿主细胞进入病毒所必需的,后者则是细胞转运过程中内质体逃逸的关键。这两个结构域都是感染所不可或缺的,因此,RBD 位于病毒的外表面,是抑制 B19V 的药物靶点。迄今为止,还没有任何 Parvovirus VP1u 成分的实验结构信息。在此,我们报告了 B19V RBD 的骨架核磁共振共振分配,并证明它形成了稳定的结构。骨架化学位移与 AlphaFold 预测的结构非常吻合,验证了 RBD 包含三个由紧密转折连接的螺旋。这种 RBD 结构现在可用于进一步的核磁共振研究,包括全长 VP1u 的分配、蛋白质-蛋白质相互作用界面的确定以及针对 RBD 结构域的 B19 抗病毒药物的开发。
{"title":"Backbone NMR resonance assignments for the VP1u N-terminal receptor-binding domain of the human parvovirus pathogen B19","authors":"Maria Luiza Caldas Nogueira,&nbsp;Renuk Lakshmanan,&nbsp;Gwladys Rivière,&nbsp;Mario Mietzsch,&nbsp;Antonette Bennett,&nbsp;Robert McKenna,&nbsp;Joanna R. Long","doi":"10.1007/s12104-024-10181-7","DOIUrl":"10.1007/s12104-024-10181-7","url":null,"abstract":"<div><p>Parvovirus B19 (B19V) is a human pathogen that is the causative agent of several diseases in infants and adults. Due to a lack of antivirals against this virus, treatment options are limited. The minor capsid protein of B19V has a unique N terminus, named VP1u, which is essential for infection. The VP1u encodes a receptor binding domain (RBD), necessary for host cell entry, and a phospholipase A2 (PLA<sub>2</sub>) domain, crucial for endosomal escape during cellular trafficking. Both domains are indispensable for infection, making the RBD a plausible drug target for inhibitors against B19V, as it is located on the exterior surface of the virus. To date, no experimental structural information has been available for the VP1u component for any Parvovirus. Here we report the backbone NMR resonance assignments for the RBD of B19V and demonstrate it forms a stable structure. The backbone chemical shifts are in good agreement with a structure predicted by AlphaFold, validating that the RBD contains three helices connected by tight turns. This RBD construct can now be used for further NMR studies, including assignment of full-length VP1u, determination of protein-protein interaction interfaces, and development of B19 antivirals specific to the RBD domain.</p></div>","PeriodicalId":492,"journal":{"name":"Biomolecular NMR Assignments","volume":null,"pages":null},"PeriodicalIF":0.8,"publicationDate":"2024-06-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141431063","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
1H, 13C and 15N backbone resonance assignment of Cel45A from Phanerochaete chrysosporium 来自 Phanerochaete chrysosporium 的 Cel45A 的 1H、13C 和 15N 主干共振分配。
IF 0.8 4区 生物学 Q4 BIOPHYSICS Pub Date : 2024-06-18 DOI: 10.1007/s12104-024-10182-6
Laura Okmane, Mats Sandgren, Jerry Ståhlberg, Gustav Nestor

A glycoside hydrolase family 45 (GH45) enzyme from the white-rot basidiomycete fungus Phanerochaete chrysosporium (PcCel45A) was expressed in Pichia pastoris with 13C and 15N labelling. A nearly complete assignment of 1H, 13C and 15N backbone resonances was obtained, as well as the secondary structure prediction based on the assigned chemical shifts using the TALOS-N software. The predicted secondary structure was almost identical to previously published crystal structures of the same enzyme, except for differences in the termini of the sequence. This is the first NMR study using an isotopically labelled GH45 enzyme.

用 13C 和 15N 标记在 Pichia pastoris 中表达了来自白腐基枝菌 Phanerochaete chrysosporium 的糖苷水解酶家族 45(GH45)(PcCel45A)。利用 TALOS-N 软件对 1H、13C 和 15N 主干共振进行了近乎完整的分配,并根据分配的化学位移对二级结构进行了预测。除了序列末端的差异外,预测的二级结构与之前公布的同一种酶的晶体结构几乎完全相同。这是首次使用同位素标记的 GH45 酶进行核磁共振研究。
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引用次数: 0
Backbone triple resonance assignments of the dimerization domain of NF-kappaB p52 subunit NF-kappaB p52 亚基二聚化结构域的骨架三重共振分配。
IF 0.8 4区 生物学 Q4 BIOPHYSICS Pub Date : 2024-06-10 DOI: 10.1007/s12104-024-10179-1
Sunirmala Sahoo, Nitin Dhaka, Sulakshana P. Mukherjee

NF-kappaB is a family of inducible transcription factors playing an important role in immune response in vertebrates. All the five members of the family function as dimers in various combinations. Though all the family members recognize and bind to similar DNA elements to regulate the transcription of its target genes, the dimer composition can lead to differential transcriptional outcomes. Here we report the backbone resonance assignment of the 24.2 kDa homodimer of p52 subunit of the NF-kB family. The p52 subunit of NF-kB is a crucial player in the non-canonical NF-kB pathway and its dysregulation has shown detrimental effects in immune response leading to various inflammatory diseases and cancers. While the β-strands predicted using the backbone chemical shifts in this study largely conform with the available crystal structure, the helical turns present in the crystal structure are not observed in our results.

NF-kappaB 是一个可诱导的转录因子家族,在脊椎动物的免疫反应中发挥着重要作用。该家族的五个成员以不同的组合形式发挥二聚体的功能。尽管所有家族成员都能识别并结合到相似的 DNA 元件上以调节其目标基因的转录,但二聚体的组成会导致不同的转录结果。在这里,我们报告了 NF-kB 家族 p52 亚基 24.2 kDa 同源二聚体的骨架共振分配。NF-kB 的 p52 亚基是非经典 NF-kB 通路中的一个重要角色,它的失调在导致各种炎症性疾病和癌症的免疫反应中显示出有害影响。虽然本研究中利用骨架化学位移预测的 β 链与现有晶体结构基本吻合,但在我们的研究结果中却没有观察到晶体结构中存在的螺旋转折。
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引用次数: 0
Resonance assignments of cytochrome MtoD from the extracellular electron uptake pathway of sideroxydans lithotrophicus ES-1 细胞色素 MtoD 的共振赋值来自于纤毛虫 ES-1 的细胞外电子摄取途径。
IF 0.8 4区 生物学 Q4 BIOPHYSICS Pub Date : 2024-06-07 DOI: 10.1007/s12104-024-10180-8
Anaísa Coelho, José M. Silva, Francesca Cantini, Mario Piccioli, Ricardo O. Louro, Catarina M. Paquete

The contribution of Fe(II)-oxidizing bacteria to iron cycling in freshwater, groundwater, and marine environments has been widely recognized in recent years. These organisms perform extracellular electron transfer (EET), which constitutes the foundations of bioelectrochemical systems for the production of biofuels and bioenergy. It was proposed that the Gram-negative bacterium Sideroxydans lithotrophicus ES-1 oxidizes soluble ferrous Fe(II) at the surface of the cell and performs EET through the Mto redox pathway. This pathway is composed by the periplasmic monoheme cytochrome MtoD that is proposed to bridge electron transfer between the cell exterior and the cytoplasm. This makes its functional and structural characterization, as well as evaluating the interaction process with its physiological partners, essential for understanding the mechanisms underlying EET. Here, we report the complete assignment of the heme proton and carbon signals together with a near-complete assignment of 1H, 13C and 15N backbone and side chain resonances for the reduced, diamagnetic form of the protein. These data pave the way to identify and structurally map the molecular interaction regions between the cytochrome MtoD and its physiological redox partners, to explore the EET processes of S. lithotrophicus ES-1.

近年来,人们广泛认识到铁(II)氧化细菌对淡水、地下水和海洋环境中铁循环的贡献。这些生物可进行胞外电子转移(EET),是生产生物燃料和生物能源的生物电化学系统的基础。有人提出,革兰氏阴性细菌 Sideroxydans lithotrophicus ES-1 在细胞表面氧化可溶性亚铁 Fe(II),并通过 Mto 氧化还原途径进行 EET。该途径由细胞质周围的单血红素细胞色素 MtoD 构成,被认为是细胞外部和细胞质之间电子传递的桥梁。因此,对其进行功能和结构鉴定,以及评估其与生理伙伴的相互作用过程,对于了解 EET 的基本机制至关重要。在此,我们报告了血红素质子和碳信号的完整分配,以及该蛋白还原二磁形式的 1H、13C 和 15N 主干和侧链共振的近乎完整的分配。这些数据为确定细胞色素 MtoD 与其生理氧化还原伙伴之间的分子相互作用区域并绘制其结构图、探索 S. lithotrophicus ES-1 的 EET 过程铺平了道路。
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引用次数: 0
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Biomolecular NMR Assignments
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