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PDBsum entry 1hfc
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Metalloprotease
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PDB id
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1hfc
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References listed in PDB file
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Key reference
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Title
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1.56 a structure of mature truncated human fibroblast collagenase.
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Authors
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J.C.Spurlino,
A.M.Smallwood,
D.D.Carlton,
T.M.Banks,
K.J.Vavra,
J.S.Johnson,
E.R.Cook,
J.Falvo,
R.C.Wahl,
T.A.Pulvino.
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Ref.
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Proteins, 1994,
19,
98.
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PubMed id
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Abstract
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The X-ray crystal structure of a 19 kDa active fragment of human fibroblast
collagenase has been determined by the multiple isomorphous replacement method
and refined at 1.56 A resolution to an R-factor of 17.4%. The current structure
includes a bound hydroxamate inhibitor, 88 waters and three metal atoms (two
zincs and a calcium). The overall topology of the enzyme, comprised of a five
stranded beta-sheet and three alpha-helices, is similar to the thermolysin-like
metalloproteinases. There are some important differences between the collagenase
and thermolysin families of enzymes. The active site zinc ligands are all
histidines (His-218, His-222, and His-228). The presence of a second zinc ion in
a structural role is a unique feature of the matrix metalloproteinases. The
binding properties of the active site cleft are more dependent on the main chain
conformation of the enzyme (and substrate) compared with thermolysin. A
mechanism of action for peptide cleavage similar to that of thermolysin is
proposed for fibroblast collagenase.
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Secondary reference #1
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Title
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Structure of human neutrophil collagenase reveals large s1' Specificity pocket.
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Authors
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T.Stams,
J.C.Spurlino,
D.L.Smith,
R.C.Wahl,
T.F.Ho,
M.W.Qoronfleh,
T.M.Banks,
B.Rubin.
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Ref.
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Nat Struct Biol, 1994,
1,
119-123.
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PubMed id
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