Crystal structure of the functional region of Uro-adherence factor A from Staphylococcus saprophyticus reveals participation of the B domain in ligand binding

Eriko Matsuoka, Yoshikazu Tanaka, Makoto Kuroda, Yuko Shouji, Toshiko Ohta, Isao Tanaka, Min Yao

Research output: Contribution to journalArticlepeer-review

9 Citations (Scopus)

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. Published by Wiley-Blackwell.

Original languageEnglish
Pages (from-to)406-416
Number of pages11
JournalProtein Science
Volume20
Issue number2
DOIs
Publication statusPublished - 2011 Feb
Externally publishedYes

Keywords

  • Crystal structure
  • Hemagglutination
  • MSCRAMMs
  • Staphylococcus saprophyticus
  • UafA

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

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