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6YZG

Streptococcal surface adhesin - CshB NR2

6YZG の概要
エントリーDOI10.2210/pdb6yzg/pdb
関連するPDBエントリー5l2d
分子名称Surface-associated protein CshB (2 entities in total)
機能のキーワードstreptococcal surface adhesin, fibronectin binding, cshb, cell adhesion
由来する生物種Streptococcus gordonii (strain Challis / ATCC 35105 / BCRC 15272 / CH1 / DL1 / V288)
タンパク質・核酸の鎖数1
化学式量合計35134.13
構造登録者
Race, P.R.,Parnell, A.E.,Barringer, R. (登録日: 2020-05-06, 公開日: 2021-05-26, 最終更新日: 2024-02-07)
主引用文献Barringer, R.,Parnell, A.E.,Lafita, A.,Monzon, V.,Back, C.R.,Madej, M.,Potempa, J.,Nobbs, A.H.,Burston, S.G.,Bateman, A.,Race, P.R.
Domain shuffling of a highly mutable ligand-binding fold drives adhesin generation across the bacterial kingdom.
Proteins, 2023
Cited by
PubMed Abstract: Bacterial fibrillar adhesins are specialized extracellular polypeptides that promote the attachment of bacteria to the surfaces of other cells or materials. Adhesin-mediated interactions are critical for the establishment and persistence of stable bacterial populations within diverse environmental niches and are important determinants of virulence. The fibronectin (Fn)-binding fibrillar adhesin CshA, and its paralogue CshB, play important roles in host colonization by the oral commensal and opportunistic pathogen Streptococcus gordonii. As paralogues are often catalysts for functional diversification, we have probed the early stages of structural and functional divergence in Csh proteins by determining the X-ray crystal structure of the CshB adhesive domain NR2 and characterizing its Fn-binding properties in vitro. Despite sharing a common fold, CshB_NR2 displays an ~1.7-fold reduction in Fn-binding affinity relative to CshA_NR2. This correlates with reduced electrostatic charge in the Fn-binding cleft. Complementary bioinformatic studies reveal that homologues of CshA/B_NR2 domains are widely distributed in both Gram-positive and Gram-negative bacteria, where they are found housed within functionally cryptic multi-domain polypeptides. Our findings are consistent with the classification of Csh adhesins and their relatives as members of the recently defined polymer adhesin domain (PAD) family of bacterial proteins.
PubMed: 36912614
DOI: 10.1002/prot.26487
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.4 Å)
構造検証レポート
Validation report summary of 6yzg
検証レポート(詳細版)ダウンロードをダウンロード

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件を2024-11-06に公開中

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