Structure features of Streptococcus pneumoniae FabG and virtual screening of allosteric inhibitors.

ABSTRACT: Streptococcus pneumoniae, a gram-positive bacterium, is responsible for diverse infections globally, and its antibiotic resistance presents significant challenges to medical advancements. It is imperative to employ various strategies to identify antibiotics. 3-oxoacyl-[acyl-carrier-protein] reductase (FabG) is a key component in the type II fatty acid synthase (FAS II) system, which is a developing target for new anti-streptococcal drugs. We first demonstrated the function of SpFabG in vivo and in vitro and the 2 Å SpFabG structure was elucidated using X-ray diffraction technique. It was observed that the NADPH binding promotes the transformation from tetramers to dimers in solution, suggesting dimers but not tetramer may be the active conformation. By comparing the st

SUBMITTER: Xu K 

PROVIDER: S-EPMC11467476 | biostudies-literature | 2024

REPOSITORIES: biostudies-literature