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3IRP

Crystal structure of functional region of UafA from Staphylococcus saprophyticus at 1.50 angstrom resolution

3IRP の概要
エントリーDOI10.2210/pdb3irp/pdb
関連するPDBエントリー3IRZ 3IS0 3IS1
分子名称Uro-adherence factor A, GLYCEROL, POTASSIUM ION, ... (4 entities in total)
機能のキーワードdev-igg fold, cell wall, hemagglutinin, peptidoglycan-anchor, secreted, virulence, cell adhesion
由来する生物種Staphylococcus saprophyticus subsp. saprophyticus
細胞内の位置Secreted, cell wall; Peptidoglycan-anchor (Potential): Q4A0V8
タンパク質・核酸の鎖数1
化学式量合計48038.07
構造登録者
Tanaka, Y.,Shouji, Y.,Matsuoka, E.,Kuroda, M.,Tanaka, I.,Yao, M. (登録日: 2009-08-24, 公開日: 2010-09-08, 最終更新日: 2023-11-01)
主引用文献Matsuoka, E.,Tanaka, Y.,Kuroda, M.,Shouji, Y.,Ohta, T.,Tanaka, I.,Yao, M.
Crystal structure of the functional region of Uro-adherence factor A from Staphylococcus saprophyticus reveals participation of the B domain in ligand binding
Protein Sci., 20:406-416, 2011
Cited by
PubMed Abstract: Staphylococci use cell wall-anchored proteins as adhesins to attach to host tissues. Staphylococcus saprophyticus, a uropathogenic species, has a unique cell wall-anchored protein, uro-adherence factor A (UafA), which shows erythrocyte binding activity. To investigate the mechanism of adhesion by UafA, we determined the crystal structure of the functional region of UafA at 1.5 Å resolution. The structure was composed of three domains, designated as the N2, N3, and B domains, arranged in a triangular relative configuration. Hemagglutination inhibition assay with domain-truncated mutants indicated that both N and B domains were necessary for erythrocyte binding. Based on these results, a novel manner of ligand binding in which the B domain acts as a functional domain was proposed as the adhesion mechanism of S. saprophyticus.
PubMed: 21280131
DOI: 10.1002/pro.573
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.5 Å)
構造検証レポート
Validation report summary of 3irp
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2025-07-23に公開中

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