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DOI | 10.2210/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: 21280131DOI: 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) |
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