biostudies-literatureZhou KChinese Academy of SciencesFundamental Research Funds for the Central UniversitiesNational Natural Science Foundation of China236-244https://www.ebi.ac.uk/biostudies/studies/S-EPMC5894109biostudies-literatureUnknown74(Pt 4)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.Acta crystallographica. Section F, Structural biology communicationsHigh-resolution crystal structure of Streptococcus agalactiae glyceraldehyde-3-phosphate dehydrogenase.PMC5894109U1732109Li YFan XJin TZhang CZhou KfalseHigh-resolution crystal structure of Streptococcus agalactiae glyceraldehyde-3-phosphate dehydrogenase.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.2018-01-01T00:00:00Z2018 Apr2025-04-19T00:29:09.385Z2020-05-22T14:54:33ZS-EPMC58941092963397210.1107/s2053230x1800380110.1107/S2053230X18003801