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

Heping Zheng, Ekaterina V Filippova, Karolina L Tkaczuk, Piotr Dworzynski, Maksymilian Chruszcz, Przemyslaw J Porebski, Zdzislaw Wawrzak, Olena Onopriyenko, Marina Kudritska, Sarah Grimshaw, Alexei Savchenko, Wayne F Anderson, Wladek Minor
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引用次数: 8

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.

Abstract Image

炭疽芽胞杆菌和空肠芽胞杆菌推定磷酸甘油酸激酶的晶体结构。
磷酸甘油酸激酶(PGK)在糖酵解厌氧葡萄糖降解和能量生成过程中不可或缺。在此,我们对来自炭疽芽孢杆菌和空肠弯曲杆菌的两个推测的PGKs进行了全面的结构分析。它们是蛋白质数据库中报道的第一批来自致病菌的PGKs。来自炭疽芽孢杆菌(BaPGK)的PGK晶体结构在1.68 Å被确定,而来自空肠弯曲杆菌(CjPGK)的PGK晶体结构在2.14 Å被确定。蛋白质的单体由两个结构域组成,每个结构域都包含一个罗斯曼折叠,通过螺旋连接在一起,螺旋可以用来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的底物和ATP结合形式相比,BaPGK和CjPGK的载脂蛋白形式均采用开放构象。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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