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Crystal structure of the functional region of Uro‐adherence factor A from Staphylococcus saprophyticus reveals participation of the B domain in ligand binding
Author(s) -
Matsuoka Eriko,
Tanaka Yoshikazu,
Kuroda Makoto,
Shouji Yuko,
Ohta Toshiko,
Tanaka Isao,
Yao Min
Publication year - 2011
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.573
Subject(s) - staphylococcus saprophyticus , domain (mathematical analysis) , ligand (biochemistry) , computational biology , chemistry , crystallography , physics , biology , staphylococcus , genetics , receptor , staphylococcus aureus , biochemistry , mathematics , bacteria , mathematical analysis
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 .