| Literature DB >> 29633972 |
Kang Zhou1, Xiaojiao Fan1, Yuelong Li1, Caiying Zhang1, Tengchuan Jin1.
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.Entities:
Keywords: NAD; Streptococcus agalactiae; asymmetric tetramer; glyceraldehyde-3-phosphate dehydrogenase; group B streptococcus; phosphate-binding sites
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Year: 2018 PMID: 29633972 PMCID: PMC5894109 DOI: 10.1107/S2053230X18003801
Source DB: PubMed Journal: Acta Crystallogr F Struct Biol Commun ISSN: 2053-230X Impact factor: 1.056