The cAMP receptor protein from Gardnerella vaginalis is not regulated by ligands.

ABSTRACT: Overgrowth of Gardnerella vaginalis causes an imbalance in vaginal microecology. The pathogenicity of G. vaginalis is directly regulated by the cAMP receptor protein (CRP). In this study, we resolve the crystal structure of CRP_Gv at a resolution of 2.22 Å and find some significant differences from homologous proteins. The first 23 amino acids of CRP_Gv are inserted into the ligand binding pocket, creating a strong steric barrier to ligand entry that has not been seen previously in its homologues. In the absence of ligands, the two α helices used by CRP_Gv to bind oligonucleotide chains are exposed and can specifically bind TGTGA-N6-TCACA sequences. cAMP and other ligands of CRP homologs are not cofactors of CRP_Gv. There is no coding gene of the ade

SUBMITTER: Dong H 

PROVIDER: S-EPMC11445507 | biostudies-literature | 2024 Oct

REPOSITORIES: biostudies-literature