4FF5

Structure basis of a novel virulence factor GHIP a glycosyl hydrolase 25 of Streptococcus pneumoniae participating in host cell invasion

4FF5 の概要

• エントリーDOI: 10.2210/pdb4ff5/pdb
• 分子名称: Glycosyl hydrolase 25, 1,2-ETHANEDIOL (3 entities in total)
• 機能のキーワード: tim fold, outer surface, hydrolase
• 由来する生物種: Streptococcus pneumoniae
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 30523.57

構造登録者

Wang, D. (登録日: 2012-05-31, 公開日: 2013-07-17, 最終更新日: 2024-02-28)

主引用文献

Niu, S.,Luo, M.,Tang, J.,Zhou, H.,Zhang, Y.,Min, X.,Cai, X.,Zhang, W.,Xu, W.,Li, D.,Ding, J.,Hu, Y.,Wang, D.,Huang, A.,Yin, Y.,Wang, D.
Structural basis of the novel S. pneumoniae virulence factor, GHIP, a glycosyl hydrolase 25 participating in host-cell invasion.
Plos One, 8:e68647-e68647, 2013

PubMed Abstract: Pathogenic bacteria produce a wide variety of virulence factors that are considered to be potential antibiotic targets. In this study, we report the crystal structure of a novel S. pneumoniae virulence factor, GHIP, which is a streptococcus-specific glycosyl hydrolase. This novel structure exhibits an α/β-barrel fold that slightly differs from other characterized hydrolases. The GHIP active site, located at the negatively charged groove in the barrel, is very similar to the active site in known peptidoglycan hydrolases. Functionally, GHIP exhibited weak enzymatic activity to hydrolyze the PNP-(GlcNAc)5 peptidoglycan by the general acid/base catalytic mechanism. Animal experiments demonstrated a marked attenuation of S. pneumoniae-mediated virulence in mice infected by ΔGHIP-deficient strains, suggesting that GHIP functions as a novel S. pneumoniae virulence factor. Furthermore, GHIP participates in allowing S. pneumoniae to colonize the nasopharynx and invade host epithelial cells. Taken together, these findings suggest that GHIP can potentially serve as an antibiotic target to effectively treat streptococcus-mediated infection.

PubMed: 23874703
DOI: 10.1371/journal.pone.0068647

実験手法

X-RAY DIFFRACTION (1.86 Å)