Crystal structure of H2-proteinase from the venom of Trimeresurus flavoviridis

Takashi Kumasaka, Masaki Yamamoto, Hideaki Moriyama, Nobuo Tanaka, Mamoru Sato, Yukiteru Katsube, Yoshio Yamakawa, Tamotsu Omori-Satoh, Sadaaki Iwanaga, Tatzuo Ueki

Research output: Contribution to journalArticlepeer-review

66 Scopus citations


The crystal structure of the zinc-protease, H2-proteinase. isolated from the venom of Trimeresurus flavoviridis has been determined. The crystallographic R factor is 0.176 for 10.635 reflections with F(obs)>2σ(F(obs)) in the 8.0 to 2.2 Å resolution range. The enzyme has two domains with a cleft in which a catalytic zinc atom is located. The N-terminal domain is composed of four helices around a central five-stranded β-sheet. The irregularly folded C-terminal domain contains one helix and two disulfide bridges. These two domains are linked by a disulfide bridge. In the zinc environment, the catalytic zinc atom forms a distorted tetrahedral coordination with three histidines and one catalytic water molecule, and the methionine-containing turn is structurally conserved. These are distinctive features of the metzincins, one of the zinc metalloprotease superfamilies. The entire structure shows good agreement with that of two Crotalus snake venom proteases, adamalysin II and atrolysin C. The H2-proteinase, however, contains no structural calcium ions, and differences of disulfide configurations and the coordination of the catalytic water molecule exist as compared with the other two proteases.

Original languageEnglish (US)
Pages (from-to)49-57
Number of pages9
JournalJournal of Biochemistry
Issue number1
StatePublished - Jan 1996
Externally publishedYes


  • Crystal structure
  • Snake venom
  • Zinc-protease

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology


Dive into the research topics of 'Crystal structure of H2-proteinase from the venom of Trimeresurus flavoviridis'. Together they form a unique fingerprint.

Cite this