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1amx
From Proteopedia
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| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 14:49:56 2007'' |
Revision as of 12:45, 30 October 2007
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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 ... [(full description)]
About this Structure
1AMX is a [Single protein] structure of sequence from [Staphylococcus aureus]. Structure known Active Site: CBR. 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
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