1HFC

1.56 ANGSTROM STRUCTURE OF MATURE TRUNCATED HUMAN FIBROBLAST COLLAGENASE

Summary for 1HFC

• Entry DOI: 10.2210/pdb1hfc/pdb
• Descriptor: FIBROBLAST COLLAGENASE, ZINC ION, CALCIUM ION, ... (5 entities in total)
• Functional Keywords: metalloprotease
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 19385.86

Authors

Spurlino, J.C.,Smith, D.L. (deposition date: 1994-09-13, release date: 1995-01-26, Last modification date: 2024-02-07)

Primary citation

Spurlino, J.C.,Smallwood, A.M.,Carlton, D.D.,Banks, T.M.,Vavra, K.J.,Johnson, J.S.,Cook, E.R.,Falvo, J.,Wahl, R.C.,Pulvino, T.A.,Wendoloski, J.J.,Smith, D.L.
1.56 A structure of mature truncated human fibroblast collagenase.
Proteins, 19:98-109, 1994

PubMed Abstract: 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.

PubMed: 8090713
DOI: 10.1002/prot.340190203

Experimental method

X-RAY DIFFRACTION (1.5 Å)