1HFC

1.56 ANGSTROM STRUCTURE OF MATURE TRUNCATED HUMAN FIBROBLAST COLLAGENASE

1HFC の概要

• エントリーDOI: 10.2210/pdb1hfc/pdb
• 分子名称: FIBROBLAST COLLAGENASE, ZINC ION, CALCIUM ION, ... (5 entities in total)
• 機能のキーワード: metalloprotease
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 19385.86

構造登録者

Spurlino, J.C.,Smith, D.L. (登録日: 1994-09-13, 公開日: 1995-01-26, 最終更新日: 2024-02-07)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.5 Å)