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Probing the role of membrane in neutralizing activity of antibodies against influenza virus 探讨膜在抗流感病毒抗体中和活性中的作用
IF 5.7 2区 生物学 Q2 BIOCHEMISTRY & MOLECULAR BIOLOGY Pub Date : 2025-12-19 DOI: 10.1016/j.str.2025.11.016
Defne G. Ozgulbas, Timothy J.C. Tan, Po-Chao Wen, Qi Wen Teo, Huibin Lv, Zhaleh Ghaemi, Martin Frank, Nicholas C. Wu, Emad Tajkhorshid
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引用次数: 0
γ-Secretase exosites as targets for substrate-selective lowering of Aβ generation γ-分泌酶外源作为底物选择性降低Aβ生成的靶点
IF 5.7 2区 生物学 Q2 BIOCHEMISTRY & MOLECULAR BIOLOGY Pub Date : 2025-12-19 DOI: 10.1016/j.str.2025.11.010
Riki Maruyama, Akio Fukumori, Satoru Funamoto, Ken Okada, Shoshin Akamine, Kanta Yanagida, Mitsuru Shinohara, Naoyuki Sato, Masayasu Okochi, Takashi Kudo, Harald Steiner
{"title":"γ-Secretase exosites as targets for substrate-selective lowering of Aβ generation","authors":"Riki Maruyama, Akio Fukumori, Satoru Funamoto, Ken Okada, Shoshin Akamine, Kanta Yanagida, Mitsuru Shinohara, Naoyuki Sato, Masayasu Okochi, Takashi Kudo, Harald Steiner","doi":"10.1016/j.str.2025.11.010","DOIUrl":"https://doi.org/10.1016/j.str.2025.11.010","url":null,"abstract":"","PeriodicalId":22168,"journal":{"name":"Structure","volume":"18 1","pages":""},"PeriodicalIF":5.7,"publicationDate":"2025-12-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145784792","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"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
An allosteric network governs Tom70 conformational dynamics to coordinate mitochondrial import 一个变构网络控制着Tom70构象动力学,以协调线粒体的输入
IF 5.7 2区 生物学 Q2 BIOCHEMISTRY & MOLECULAR BIOLOGY Pub Date : 2025-12-11 DOI: 10.1016/j.str.2025.11.011
Maxwell J. Bachochin, Kelly L. McGuire, Brian D. Cook, Qiaozhen Ye, Steven Silletti, Kevin D. Corbett, Elizabeth A. Komives, Mark A. Herzik
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引用次数: 0
Cryo-EM structure of cyanopodophage Pan3 reveals a modular tail architecture for host recognition 噬藻体Pan3的低温电镜结构揭示了一个用于宿主识别的模块化尾部结构
IF 5.7 2区 生物学 Q2 BIOCHEMISTRY & MOLECULAR BIOLOGY Pub Date : 2025-12-10 DOI: 10.1016/j.str.2025.11.012
Pu Hou, Jie Zhu, Rong-Cheng Yu, Feng Yang, Kang Du, Jing Li, Wen-Wen Kong, Jie Wang, Yuxing Chen, Cong-Zhao Zhou, Yong-Liang Jiang
Cyanophages, which are bacteriophages that specifically infect host cyanobacteria, also utilize the tail to initiate host recognition and adsorption. Owing to the limited structural information on cyanophages, our understanding of the mechanism by which cyanophages specifically recognize their hosts remains largely unknown. Here, we determined the intact cryoelectron microscopy structure of a freshwater cyanopodophage Pan3, which consists of an icosahedral shell and a short tail comprising four modular components: the dodecameric adaptor, hexameric nozzle, trimeric needle, and six heterohexameric tailspikes. Notably, each tailspike features an SGNH esterase domain fused to a lectin domain, forming a continuous groove complementary to the host lipopolysaccharide. These findings provide insights into the receptor engagement in Podoviridae, and establish a structural framework for cyanophage and host interactions that may guide future antibacterial interventions against harmful blooms.
噬藻体是一种专门感染宿主蓝藻的噬菌体,它也利用尾巴来启动宿主识别和吸附。由于对噬藻体的结构信息有限,我们对噬藻体特异性识别宿主的机制的理解仍然很大程度上是未知的。在这里,我们确定了淡水藻噬体Pan3的完整冷冻电镜结构,它由一个二十面体外壳和一个短尾组成,短尾由四个模块组成:十二聚体接头、六聚体喷嘴、三聚体针和六个异六聚体尾刺。值得注意的是,每个尾穗都有一个与凝集素结构域融合的SGNH酯酶结构域,形成一个与宿主脂多糖互补的连续凹槽。这些发现提供了对Podoviridae中受体参与的见解,并建立了一个噬藻体和宿主相互作用的结构框架,可能指导未来针对有害华花的抗菌干预。
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引用次数: 0
Amyloid-motif-dependent tau self-assembly is modulated by isoform sequence context 淀粉样蛋白基序依赖的tau蛋白自组装受到同种异构体序列背景的调节
IF 5.7 2区 生物学 Q2 BIOCHEMISTRY & MOLECULAR BIOLOGY Pub Date : 2025-12-05 DOI: 10.1016/j.str.2025.11.009
The microtubule-associated protein tau is implicated in neurodegenerative diseases characterized by amyloid formation. Mutations associated with front…
微管相关蛋白tau与以淀粉样蛋白形成为特征的神经退行性疾病有关。与前…相关的突变
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引用次数: 0
Rethinking what pLDDT really tells us about protein flexibility. 重新思考pLDDT到底告诉了我们什么关于蛋白质的灵活性。
IF 5.7 2区 生物学 Q2 BIOCHEMISTRY & MOLECULAR BIOLOGY Pub Date : 2025-12-04 DOI: 10.1016/j.str.2025.11.008
Jakob R Riccabona,Johannes R Loeffler,Clara T Schoeder,Jens Meiler,Andrew B Ward,Monica Fernandez-Quintero
Deep-learning models have transformed structural biology by enabling reliable prediction of protein 3D structure models and providing confidence metrics such as predicted local distance difference test (pLDDT) to estimate local uncertainties. However, whether pLDDT reflects intrinsic protein flexibility remains unclear. Defining and quantifying flexibility and protein dynamics through experiments and computation is essential for advancing our ability to model and interpret conformational changes across different timescales.
深度学习模型通过可靠地预测蛋白质3D结构模型和提供预测局部距离差测试(pLDDT)等置信度指标来估计局部不确定性,从而改变了结构生物学。然而,pLDDT是否反映了蛋白质的内在灵活性尚不清楚。通过实验和计算来定义和量化灵活性和蛋白质动力学对于提高我们在不同时间尺度上建模和解释构象变化的能力至关重要。
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引用次数: 0
Capture first, then deliver! 先抓,再送!
IF 4.3 2区 生物学 Q2 BIOCHEMISTRY & MOLECULAR BIOLOGY Pub Date : 2025-12-04 DOI: 10.1016/j.str.2025.11.001
Iktae Kim, Jeong-Yong Suh

In this issue of Structure, Henriques et al.1 present structural snapshots that capture distinct conformational states of the type I-F Cas1-Cas2/3 integrase complex, illustrating that foreign DNA binding triggers a large-scale domain rearrangement that enables prespacer delivery to the CRISPR array.

在本期《结构》杂志中,Henriques等人1展示了捕捉I-F型Cas1-Cas2/3整合酶复合体不同构象状态的结构快照,说明外源DNA结合触发大规模结构域重排,从而使预间隔物能够传递到CRISPR阵列。
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引用次数: 0
Our authors in 2025. 我们的作者在2025年。
IF 4.3 2区 生物学 Q2 BIOCHEMISTRY & MOLECULAR BIOLOGY Pub Date : 2025-12-04 DOI: 10.1016/j.str.2025.11.007
Kate L White, Jin Young Kang, Renhong Yan, Katherine M Davis, Qianglin Fang, Lorena Saelices Gomez, Anthony W P Fitzpatrick, Mohammad T Mazhab-Jafari, Tatiana Galochkina

As 2025 comes to an end, we want to highlight some of the rising young faculty members who have published their exciting work from different areas of structural biology in Structure this year. We have asked them to tell us more about their interests, careers, and research programs.

在2025年即将结束之际,我们想重点介绍一些正在崛起的年轻教师,他们在今年的《结构》杂志上发表了来自结构生物学不同领域的令人兴奋的研究成果。我们要求他们告诉我们更多关于他们的兴趣、职业和研究项目。
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引用次数: 0
Cryo-EM structure of drug-resistant Escherichia coli phage E1004 reveals a conserved cylindrical core among podophages 耐药大肠杆菌噬菌体E1004的低温电镜结构揭示了噬菌体中保守的圆柱形核
IF 5.7 2区 生物学 Q2 BIOCHEMISTRY & MOLECULAR BIOLOGY Pub Date : 2025-11-28 DOI: 10.1016/j.str.2025.11.006
Binning Sun, Jing Zheng, Yuan Fu, Fengyuan Tian, Hao Xiao, Su Li, Lingpeng Cheng, Ping Chen, Hongrong Liu
Podophage tails are too short to traverse the cell envelope and require internal core proteins to assemble into a transmembrane channel for genome delivery during infection. However, high-resolution structures of near-complete cores remain scarce. Here, we present the near-atomic-resolution cryo-electron microscopy (cryo-EM) structure of the drug-resistant E. coli phage E1004, which features a T7-like core-portal-tail structure with six P22-like tailspikes. We found that the cylindrical core comprises four proteins: gp17, gp27, gp28, and gp29. Gp29 forms a tetramer, while gp28 and gp27 assemble into octamers. Notably, there are sixteen copies of gp17 in two conformations, distinct from the small core protein gp6.7 in T7. The gp17-gp27 complex reveals the mechanism for mediating the symmetry adjustment at the core-portal interface. Moreover, comparative analysis with other podophage cores highlights diversity in core protein composition and organization, particularly among the small core proteins. We propose that these variations represent evolutionary adaptations to diverse host envelopes.
足噬体尾部太短,无法穿过细胞包膜,需要内部核心蛋白组装成跨膜通道,以便在感染期间传递基因组。然而,接近完整岩心的高分辨率结构仍然很少。在这里,我们展示了耐药大肠杆菌噬菌体E1004的近原子分辨率低温电镜(cro - em)结构,它具有t7样的核心-门户-尾部结构,具有6个p22样的尾尖。我们发现圆柱形核包含四种蛋白质:gp17, gp27, gp28和gp29。Gp29形成四聚体,gp28和gp27组装成八聚体。值得注意的是,gp17有两种构象的16个拷贝,与T7中的小核心蛋白gp6.7不同。gp17-gp27复合物揭示了介导核-门脉界面对称调节的机制。此外,与其他podophage核心的比较分析突出了核心蛋白组成和组织的多样性,特别是在小核心蛋白之间。我们认为这些变异代表了对不同寄主包膜的进化适应。
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引用次数: 0
The therapeutic antibody sacituzumab induces trophoblast cell-surface antigen-2 conformational rearrangement 治疗性抗体sacituzumab诱导滋养细胞表面抗原-2构象重排
IF 5.7 2区 生物学 Q2 BIOCHEMISTRY & MOLECULAR BIOLOGY Pub Date : 2025-11-27 DOI: 10.1016/j.str.2025.11.002
Ryan Ferrao, Jinjin Zhang, Chih-Chien Chou, Anthony Nieto, Derek Langeslay, Moon Chatterjee, Debi Jin, Magdeleine Hung, Ian Scott, Mark Nagel, Weimei Xing, Simon Letarte, Jenny Wang, Alexandre Ambrogelly, Eric B. Lansdon
Sacituzumab govitecan (SG) is a therapeutic antibody-drug conjugate globally approved for the treatment of breast cancer. SG targets the trophoblast cell-surface antigen-2 (Trop2) at the surface of cancer cells to deliver the cytotoxic topoisomerase I inhibitor SN-38 to the tumor microenvironment. SN-38 is covalently linked to the humanized monoclonal antibody (mAb) sacituzumab via a hydrolyzable linker. Here, we describe the 1.56-Å X-ray crystal structure and stoichiometry of the human Trop2 ectodomain in complex with a sacituzumab (hRS7) antigen-binding Fab fragment. The complex reveals a 2:2 stoichiometry where two sacituzumab Fabs bind across the two Trop2 dimer subunits, inducing a conformational change compared to the apo-structure. Cryo-electron microscopy (cryoEM) and size-exclusion chromatography in combination with multi-angle light scattering (SEC-MALS) analysis of the intact sacituzumab mAb bound to the Trop2 ECD reveals a complex whereby sacituzumab engages two Trop2 dimers in a 2:4 stoichiometry.
Sacituzumab govitecan (SG)是一种全球批准用于治疗乳腺癌的治疗性抗体-药物偶联物。SG靶向癌细胞表面的滋养细胞表面抗原-2 (trophoblast cell-surface antigen-2, Trop2),将细胞毒性拓扑异构酶I抑制剂SN-38传递到肿瘤微环境。SN-38通过可水解的连接物与人源化单克隆抗体sacituzumab共价连接。在这里,我们描述了人类Trop2外结构域与sacituzumab (hRS7)抗原结合Fab片段复合物的1.56-Å x射线晶体结构和化学计量学。该复合物显示出2:2的化学计量,其中两个sacituzumab fab结合在两个Trop2二聚体亚基上,诱导与载脂蛋白结构相比的构象变化。冷冻电子显微镜(cryoEM)和尺寸排除色谱结合多角度光散射(SEC-MALS)分析了与Trop2 ECD结合的完整的sacituzumab单抗,揭示了一个复合物,其中sacituzumab以2:4的化学计量与两个Trop2二聚体结合。
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引用次数: 0
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Structure
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