This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1amx
From Proteopedia
| Line 5: | Line 5: | ||
==Overview== | ==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 . | + | 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== | ==About this Structure== | ||
| - | 1AMX is a | + | 1AMX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Structure known Active Site: CBR. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AMX OCA]. |
==Reference== | ==Reference== | ||
| Line 19: | Line 19: | ||
[[Category: mscramm]] | [[Category: mscramm]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 13:34:28 2007'' |
Revision as of 11:29, 5 November 2007
|
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. 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
Page seeded by OCA on Mon Nov 5 13:34:28 2007
