A preliminary X-ray study of transketolase from Burkholderia pseudomallei.

Mi Sun Kim, Areum Lim, Seung Won Yang, Daeun Lee, Jimin Park, Dong Hae Shin
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Abstract

TktA is the most critical enzyme in the nonoxidative pentose phosphate pathway. It catalyzes the conversion of xylulose 5-phosphate and ribose 5-phosphate into sedoheptulose 7-phosphate and glyceraldehyde 3-phosphate, and its products are used in the biosynthesis of acetyl-CoA, aromatic amino acids, nucleic acids and ADP-L-glycero-β-D-manno-heptose. TktA also has an unexpected role in chromosome structure that is independent of its metabolic responsibilities. Therefore, it is a new potent antibiotic target. In this study, TktA from Burkholderia pseudomallei has been cloned, expressed, purified and crystallized. Synchrotron X-ray data were also collected to 2.0 Å resolution. The crystal belonged to the monoclinic space group C2, with unit-cell parameters a=146.2, b=74.6, c=61.6 Å, β=113.0°. A full structural determination is under way in order to provide insight into the structure-function relationship of this protein.

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假马勒伯克霍尔德氏菌转酮醇酶的 X 射线初步研究。
TktA 是磷酸戊糖非氧化途径中最关键的酶。它催化 5-磷酸木酮糖和 5-磷酸核糖转化为 7-磷酸色酮糖和 3-磷酸甘油醛,其产物用于乙酰-CoA、芳香族氨基酸、核酸和 ADP-L-甘油-β-D-甘露庚糖的生物合成。TktA 还在染色体结构中发挥着意想不到的作用,这种作用与其代谢责任无关。因此,它是一个新的强效抗生素靶标。本研究克隆、表达、纯化和结晶了假马来伯克霍尔德菌中的 TktA。研究还收集了分辨率为 2.0 Å 的同步辐射 X 射线数据。晶体属于单斜空间群 C2,单胞参数 a=146.2、b=74.6、c=61.6 Å、β=113.0°。目前正在进行全面的结构测定,以便深入了解这种蛋白质的结构与功能关系。
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期刊介绍: Acta Crystallographica Section F is a rapid structural biology communications journal. Articles on any aspect of structural biology, including structures determined using high-throughput methods or from iterative studies such as those used in the pharmaceutical industry, are welcomed by the journal. The journal offers the option of open access, and all communications benefit from unlimited free use of colour illustrations and no page charges. Authors are encouraged to submit multimedia content for publication with their articles. Acta Cryst. F has a dedicated online tool called publBio that is designed to make the preparation and submission of articles easier for authors.
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