Structure of the collagen-binding domain from a Staphylococcus aureus adhesin.
Nat Struct Biol
; 4(10): 833-8, 1997 Oct.
Article
en En
| MEDLINE
| ID: mdl-9334749
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.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Colágeno
/
Estructura Secundaria de Proteína
/
Pliegue de Proteína
/
Adhesinas Bacterianas
Idioma:
En
Revista:
Nat Struct Biol
Asunto de la revista:
BIOLOGIA MOLECULAR
Año:
1997
Tipo del documento:
Article
País de afiliación:
Estados Unidos
Pais de publicación:
Estados Unidos