1amx
From Proteopedia
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COLLAGEN-BINDING DOMAIN FROM A STAPHYLOCOCCUS AUREUS ADHESIN
Overview
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.
About this Structure
1AMX is a Single protein structure of sequence from Staphylococcus aureus. Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
Structure of the collagen-binding domain from a Staphylococcus aureus adhesin., Symersky J, Patti JM, Carson M, House-Pompeo K, Teale M, Moore D, Jin L, Schneider A, DeLucas LJ, Hook M, Narayana SV, Nat Struct Biol. 1997 Oct;4(10):833-8. PMID:9334749
Page seeded by OCA on Thu Feb 21 11:46:16 2008
