8HM3
Complex of PPIase-BfUbb
8HM3 の概要
| エントリーDOI | 10.2210/pdb8hm3/pdb |
| 分子名称 | Putative ubiquitin, Peptidylprolyl isomerase, GLYCEROL, ... (6 entities in total) |
| 機能のキーワード | isomerase, human ubiquitin-like protein |
| 由来する生物種 | Bacteroides fragilis 詳細 |
| タンパク質・核酸の鎖数 | 4 |
| 化学式量合計 | 116935.17 |
| 構造登録者 | |
| 主引用文献 | Jiang, K.,Li, W.,Tong, M.,Xu, J.,Chen, Z.,Yang, Y.,Zang, Y.,Jiao, X.,Liu, C.,Lim, B.,Jiang, X.,Wang, J.,Wu, D.,Wang, M.,Liu, S.J.,Shao, F.,Gao, X. Bacteroides fragilis ubiquitin homologue drives intraspecies bacterial competition in the gut microbiome. Nat Microbiol, 9:70-84, 2024 Cited by PubMed Abstract: Interbacterial antagonism and associated defensive strategies are both essential during bacterial competition. The human gut symbiont Bacteroides fragilis secretes a ubiquitin homologue (BfUbb) that is toxic to a subset of B. fragilis strains in vitro. In the present study, we demonstrate that BfUbb lyses certain B. fragilis strains by non-covalently binding and inactivating an essential peptidyl-prolyl isomerase (PPIase). BfUbb-sensitivity profiling of B. fragilis strains revealed a key tyrosine residue (Tyr119) in the PPIase and strains that encode a glutamic acid residue at Tyr119 are resistant to BfUbb. Crystal structural analysis and functional studies of BfUbb and the BfUbb-PPIase complex uncover a unique disulfide bond at the carboxy terminus of BfUbb to mediate the interaction with Tyr119 of the PPIase. In vitro coculture assays and mouse studies show that BfUbb confers a competitive advantage for encoding strains and this is further supported by human gut metagenome analyses. Our findings reveal a previously undescribed mechanism of bacterial intraspecies competition. PubMed: 38082149DOI: 10.1038/s41564-023-01541-5 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.26 Å) |
構造検証レポート
検証レポート(詳細版)
をダウンロード






