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PDBsum entry 1amx
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Bacterial adhesin
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PDB id
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1amx
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References listed in PDB file
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Key reference
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Title
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Structure of the collagen-Binding domain from a staphylococcus aureus adhesin.
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Authors
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J.Symersky,
J.M.Patti,
M.Carson,
K.House-Pompeo,
M.Teale,
D.Moore,
L.Jin,
A.Schneider,
L.J.Delucas,
M.Höök,
S.V.Narayana.
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Ref.
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Nat Struct Biol, 1997,
4,
833-838.
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PubMed id
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Abstract
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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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