1AMX

COLLAGEN-BINDING DOMAIN FROM A STAPHYLOCOCCUS AUREUS ADHESIN

Summary for 1AMX

• Entry DOI: 10.2210/pdb1amx/pdb
• Descriptor: COLLAGEN ADHESIN (2 entities in total)
• Functional Keywords: bacterial adhesin, mscramm
• Biological source: Staphylococcus aureus
• Cellular location: Secreted, cell wall; Peptidoglycan-anchor (Potential): Q53654
• Total number of polymer chains: 1
• Total formula weight: 20314.10

Authors

Symersky, J.,Narayana, S. (deposition date: 1997-06-19, release date: 1998-06-24, Last modification date: 2024-02-07)

Primary citation

Symersky, J.,Patti, J.M.,Carson, M.,House-Pompeo, K.,Teale, M.,Moore, D.,Jin, L.,Schneider, A.,DeLucas, L.J.,Hook, M.,Narayana, S.V.
Structure of the collagen-binding domain from a Staphylococcus aureus adhesin.
Nat.Struct.Biol., 4:833-838, 1997

PubMed Abstract: The crystal structure of the recombinant 19,000 M(r) binding domain from the Staphylococcus aureus collagen adhesin has been determined at 2 A resolution. The domain fold is a jelly-roll, composed of two antiparallel beta-sheets and two short alpha-helices. Triple-helical collagen model probes were used in a systematic docking search to identify the collagen-binding site. A groove on beta-sheet I exhibited the best surface complementarity to the collagen probes. This site partially overlaps with the peptide sequence previously shown to be critical for collagen binding. Recombinant proteins containing single amino acid mutations designed to disrupt the surface of the putative binding site exhibited significantly lower affinities for collagen. Here we present a structural perspective for the mode of collagen binding by a bacterial surface protein.

PubMed: 9334749
DOI: 10.1038/nsb1097-833

Experimental method

X-RAY DIFFRACTION (2 Å)