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炭疽芽孢杆菌和空肠弯曲菌中假定磷酸甘油酸激酶的晶体结构。

Crystal structures of putative phosphoglycerate kinases from B. anthracis and C. jejuni.

作者信息

Zheng Heping, Filippova Ekaterina V, Tkaczuk Karolina L, Dworzynski Piotr, Chruszcz Maksymilian, Porebski Przemyslaw J, Wawrzak Zdzislaw, Onopriyenko Olena, Kudritska Marina, Grimshaw Sarah, Savchenko Alexei, Anderson Wayne F, Minor Wladek

机构信息

Department of Molecular Physiology and Biological Physics, University of Virginia, 1340 Jefferson Park Avenue, Charlottesville, VA 22908, USA.

出版信息

J Struct Funct Genomics. 2012 Mar;13(1):15-26. doi: 10.1007/s10969-012-9131-9. Epub 2012 Mar 10.

DOI:10.1007/s10969-012-9131-9
PMID:22403005
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC4485498/
Abstract

Phosphoglycerate kinase (PGK) is indispensable during glycolysis for anaerobic glucose degradation and energy generation. Here we present comprehensive structure analysis of two putative PGKs from Bacillus anthracis str. Sterne and Campylobacter jejuni in the context of their structural homologs. They are the first PGKs from pathogenic bacteria reported in the Protein Data Bank. The crystal structure of PGK from Bacillus anthracis str. Sterne (BaPGK) has been determined at 1.68 Å while the structure of PGK from Campylobacter jejuni (CjPGK) has been determined at 2.14 Å resolution. The proteins' monomers are composed of two domains, each containing a Rossmann fold, hinged together by a helix which can be used to adjust the relative position between two domains. It is also shown that apo-forms of both BaPGK and CjPGK adopt open conformations as compared to the substrate and ATP bound forms of PGK from other species.

摘要

磷酸甘油酸激酶(PGK)在糖酵解过程中对于厌氧葡萄糖降解和能量生成不可或缺。在此,我们结合其结构同源物,对炭疽芽孢杆菌斯特恩菌株和空肠弯曲菌中的两种假定PGK进行了全面的结构分析。它们是蛋白质数据库中报道的首批来自病原菌的PGK。炭疽芽孢杆菌斯特恩菌株的PGK(BaPGK)晶体结构已在1.68 Å分辨率下确定,而空肠弯曲菌的PGK(CjPGK)结构已在2.14 Å分辨率下确定。蛋白质单体由两个结构域组成,每个结构域都含有一个罗斯曼折叠,通过一个螺旋连接在一起,该螺旋可用于调节两个结构域之间的相对位置。研究还表明,与其他物种的PGK底物和ATP结合形式相比,BaPGK和CjPGK的无配体形式均采用开放构象。

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