4GSO

structure of Jararacussin-I

4GSO の概要

• エントリーDOI: 10.2210/pdb4gso/pdb
• 分子名称: Thrombin-like enzyme BjussuSP-1 (2 entities in total)
• 機能のキーワード: thrombin-like enzyme, hydrolase
• 由来する生物種: Bothrops jararacussu (Jararacussu)
• 細胞内の位置: Secreted: Q2PQJ3
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 25183.45

構造登録者

Ullah, A.,Souza, T.C.A.B.,Zanphorlin, L.M.,Mariutti, R.,Sanata, S.V.,Murakami, M.T.,Arni, R.K. (登録日: 2012-08-28, 公開日: 2012-12-12, 最終更新日: 2024-10-16)

主引用文献

Ullah, A.,Souza, T.A.,Zanphorlin, L.M.,Mariutti, R.B.,Santana, V.S.,Murakami, M.T.,Arni, R.K.
Crystal structure of Jararacussin-I: The highly negatively charged catalytic interface contributes to macromolecular selectivity in snake venom thrombin-like enzymes.
Protein Sci., 22:128-132, 2013

PubMed Abstract: Snake venom serine proteinases (SVSPs) are hemostatically active toxins that perturb the maintenance and regulation of both the blood coagulation cascade and fibrinolytic feedback system at specific points, and hence, are widely used as tools in pharmacological and clinical diagnosis. The crystal structure of a thrombin-like enzyme (TLE) from Bothrops jararacussu venom (Jararacussin-I) was determined at 2.48 Å resolution. This is the first crystal structure of a TLE and allows structural comparisons with both the Agkistrodon contortrix contortrix Protein C Activator and the Trimeresurus stejnegeri plasminogen activator. Despite the highly conserved overall fold, significant differences in the amino acid compositions and three-dimensional conformations of the loops surrounding the active site significantly alter the molecular topography and charge distribution profile of the catalytic interface. In contrast to other SVSPs, the catalytic interface of Jararacussin-I is highly negatively charged, which contributes to its unique macromolecular selectivity.

PubMed: 23139169
DOI: 10.1002/pro.2189

実験手法

X-RAY DIFFRACTION (2.6 Å)