Structure of the collagen-binding domain from a Staphylococcus aureus adhesin

Jindrich Symersky; Joseph M. Patti; Mike Carson; Karen House-Pompeo; Michael Teale; Dwight Moore; Lei Jin; Amy Schneider; Lawrence J. Delucas; Magnus Hook; Sthanam V.L. Narayana

doi:10.1038/nsb1097-833

Structure of the collagen-binding domain from a Staphylococcus aureus adhesin

Jindrich Symersky, Joseph M. Patti, Mike Carson, Karen House-Pompeo, Michael Teale, Dwight Moore, Lei Jin, Amy Schneider, Lawrence J. Delucas, Magnus Hook, Sthanam V.L. Narayana

Research Institute

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123 Scopus citations

Abstract

The crystal structure of the recombinant 19,000 M, 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 β-sheets and two short α-helices. Triple-helical collagen model probes were used in a systematic docking search to identify the collagen-binding site. A groove on β-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.

Original language	English (US)
Pages (from-to)	833-838
Number of pages	6
Journal	Nature Structural Biology
Volume	4
Issue number	10
DOIs	https://doi.org/10.1038/nsb1097-833
State	Published - 1997

ASJC Scopus subject areas

Structural Biology
Biochemistry
Genetics

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abstract = "The crystal structure of the recombinant 19,000 M, 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 β-sheets and two short α-helices. Triple-helical collagen model probes were used in a systematic docking search to identify the collagen-binding site. A groove on β-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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AU - Symersky, Jindrich

AU - Patti, Joseph M.

AU - Carson, Mike

AU - House-Pompeo, Karen

AU - Teale, Michael

AU - Moore, Dwight

AU - Jin, Lei

AU - Schneider, Amy

AU - Delucas, Lawrence J.

AU - Hook, Magnus

AU - Narayana, Sthanam V.L.

PY - 1997

Y1 - 1997

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AB - The crystal structure of the recombinant 19,000 M, 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 β-sheets and two short α-helices. Triple-helical collagen model probes were used in a systematic docking search to identify the collagen-binding site. A groove on β-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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Structure of the collagen-binding domain from a Staphylococcus aureus adhesin

Abstract

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