1IAG

FIRST STRUCTURE OF A SNAKE VENOM METALLOPROTEINASE: A PROTOTYPE FOR MATRIX METALLOPROTEINASES(SLASH)COLLAGENASES

1IAG の概要

• エントリーDOI: 10.2210/pdb1iag/pdb
• 分子名称: ADAMALYSIN II, ZINC ION, CALCIUM ION, ... (5 entities in total)
• 機能のキーワード: metalloprotease
• 由来する生物種: Crotalus adamanteus (eastern diamondback rattlesnake)
• 細胞内の位置: Secreted: P34179
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 23413.19

構造登録者

Gomis-Rueth, F.-X.,Bode, W. (登録日: 1994-05-09, 公開日: 1994-08-31, 最終更新日: 2024-10-30)

主引用文献

Gomis-Ruth, F.X.,Kress, L.F.,Bode, W.
First structure of a snake venom metalloproteinase: a prototype for matrix metalloproteinases/collagenases.
EMBO J., 12:4151-4157, 1993

PubMed Abstract: Adamalysin II, a 24 kDa zinc endopeptidase from the snake venom of Crotalus adamanteus, is a member of a large family of metalloproteinases isolated as small proteinases or proteolytic domains of mosaic haemorrhagic proteins from various snake venoms. Homologous domains have recently been detected in multimodular mammalian reproductive tract proteins. The 2.0 A crystal structure of adamalysin II reveals an ellipsoidal molecule with a shallow active-site cleft separating a relatively irregularly folded subdomain from the calcium-binding main molecular body composed of a five-stranded beta-sheet and four alpha-helices. The folding of the peptide fragment containing the zinc-binding motif HExxHxxGxxH bears only a distant resemblance to thermolysin, but is identical to that found in astacin, with the three histidines and a water molecule (linked to the glutamic acid) likewise constituting the zinc ligand; adamalysin II lacks a fifth (tyrosine) zinc ligand, however, leaving its zinc ion tetrahedrally co-ordinated. Furthermore, adamalysin II and astacin share an identical active-site basement formed by a common Metturn. Due to their virtually identical active-site environment and similar folding topology, the snake venom metalloproteinases (hitherto called adamalysins) and the astacins (and presumably also the matrix metalloproteinases/mammalian collagenases and the Serratia proteinase-like large bacterial proteinases) might be grouped into a common superfamily with distinct differences from the thermolysin family.

PubMed: 8223430

実験手法

X-RAY DIFFRACTION (2 Å)