3IS1

Crystal structure of functional region of UafA from Staphylococcus saprophyticus in C2 form at 2.45 angstrom resolution

Summary for 3IS1

• Entry DOI: 10.2210/pdb3is1/pdb
• Related: 3IRP 3IRZ 3IS0
• Descriptor: Uro-adherence factor A, GLYCEROL (3 entities in total)
• Functional Keywords: dev-igg fold, cell wall, hemagglutinin, peptidoglycan-anchor, secreted, virulence, cell adhesion
• Biological source: Staphylococcus saprophyticus subsp. saprophyticus
• Cellular location: Secreted, cell wall; Peptidoglycan-anchor (Potential): Q4A0V8
• Total number of polymer chains: 1
• Total formula weight: 49603.46

Authors

Tanaka, Y.,Matsuoka, E.,Shouji, Y.,Kuroda, M.,Tanaka, I.,Yao, M. (deposition date: 2009-08-24, release date: 2010-09-08, Last modification date: 2024-03-20)

Primary citation

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

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

Experimental method

X-RAY DIFFRACTION (2.45 Å)