无乳链球菌3-磷酸甘油醛脱氢酶的高分辨率晶体结构
High-resolution crystal structure of Streptococcus agalactiae glyceraldehyde-3-phosphate dehydrogenase.
作者信息
Zhou Kang, Fan Xiaojiao, Li Yuelong, Zhang Caiying, Jin Tengchuan
机构信息
Laboratory of Structural Immunology, CAS Key Laboratory of Innate Immunity and Chronic Disease, CAS Center for Excellence in Molecular Cell Science, School of Life Sciences and Medical Center, University of Science and Technology of China, Hefei, Anhui 230027, People's Republic of China.
出版信息
Acta Crystallogr F Struct Biol Commun. 2018 Apr 1;74(Pt 4):236-244. doi: 10.1107/S2053230X18003801. Epub 2018 Mar 23.
Abstract
Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a multifunctional enzyme that plays critical roles in bacterial pathogenesis in some pathogenic bacteria. In this study, the crystal structure of group B streptococcus GAPDH was determined at 1.36 Å resolution. The structure contained an asymmetric mixed holo tetramer, with two NAD ligands bound to two protomers. Further structural analysis identified interesting phosphate ion-binding sites, which shed light on its catalytic mechanism.
摘要
甘油醛-3-磷酸脱氢酶（GAPDH）是一种多功能酶，在某些病原菌的细菌致病过程中发挥关键作用。在本研究中，B族链球菌GAPDH的晶体结构在1.36 Å分辨率下得以确定。该结构包含一个不对称的混合全四聚体，有两个NAD配体与两个原体结合。进一步的结构分析确定了有趣的磷酸根离子结合位点，这为其催化机制提供了线索。
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