无乳链球菌甘油醛-3-磷酸脱氢酶全酶的结构揭示了一个新的表面。
Structure of Streptococcus agalactiae glyceraldehyde-3-phosphate dehydrogenase holoenzyme reveals a novel surface.
作者信息
Ayres Chapelle A, Schormann Norbert, Senkovich Olga, Fry Alexandra, Banerjee Surajit, Ulett Glen C, Chattopadhyay Debasish
机构信息
Science and Technology Honors Program, University of Alabama at Birmingham, Birmingham, AL 35294, USA.
Center for Biophysical Sciences and Engineering, University of Alabama at Birmingham, Birmingham, AL 35294, USA.
出版信息
Acta Crystallogr F Struct Biol Commun. 2014 Oct;70(Pt 10):1333-9. doi: 10.1107/S2053230X14019517. Epub 2014 Sep 25.
Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a conserved cytosolic enzyme, which plays a key role in glycolysis. GAPDH catalyzes the oxidative phosphorylation of D-glyceraldehyde 3-phosphate using NAD or NADP as a cofactor. In addition, GAPDH localized on the surface of some bacteria is thought to be involved in macromolecular interactions and bacterial pathogenesis. GAPDH on the surface of group B streptococcus (GBS) enhances bacterial virulence and is a potential vaccine candidate. Here, the crystal structure of GBS GAPDH from Streptococcus agalactiae in complex with NAD is reported at 2.46 Å resolution. Although the overall structure of GBS GAPDH is very similar to those of other GAPDHs, the crystal structure reveals a significant difference in the area spanning residues 294-307, which appears to be more acidic. The amino-acid sequence of this region of GBS GAPDH is also distinct compared with other GAPDHs. This region therefore may be of interest as an immunogen for vaccine development.
甘油醛-3-磷酸脱氢酶（GAPDH）是一种保守的胞质酶，在糖酵解过程中起关键作用。GAPDH以NAD或NADP作为辅因子催化D-甘油醛3-磷酸的氧化磷酸化。此外，定位于某些细菌表面的GAPDH被认为参与大分子相互作用和细菌致病过程。B族链球菌（GBS）表面的GAPDH可增强细菌毒力，是一种潜在的疫苗候选物。在此，报道了无乳链球菌GBS GAPDH与NAD复合物的晶体结构，分辨率为2.46 Å。尽管GBS GAPDH的整体结构与其他GAPDH非常相似，但晶体结构显示在跨越残基294 - 307的区域存在显著差异，该区域似乎酸性更强。与其他GAPDH相比，GBS GAPDH该区域的氨基酸序列也不同。因此，该区域作为疫苗开发的免疫原可能具有研究价值。
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