6X5X

Crystal structure o BmooMP-I, a P-I metalloproteinase from Bothrops moojeni

6X5X の概要

• エントリーDOI: 10.2210/pdb6x5x/pdb
• 分子名称: Snake venom metalloproteinase BmooMP-I, CALCIUM ION, ZINC ION, ... (6 entities in total)
• 機能のキーワード: metalloproteinase p-i, fibrinogenolytic metalloproteinase, hydrolase
• 由来する生物種: Bothrops moojeni
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 23066.32

構造登録者

Salvador, G.H.M.,Borges, R.J.,Fontes, M.R.M. (登録日: 2020-05-27, 公開日: 2020-10-07, 最終更新日: 2024-11-06)

主引用文献

Salvador, G.H.M.,Borges, R.J.,Eulalio, M.M.C.,Dos Santos, L.D.,Fontes, M.R.M.
Biochemical, pharmacological and structural characterization of BmooMP-I, a new P-I metalloproteinase from Bothrops moojeni venom.
Biochimie, 179:54-64, 2020

PubMed Abstract: Snakebite envenoming is still a worrying health problem in countries under development, being recognized as a neglected disease by the World Health Organization. In Latin America, snakes from the genus Bothrops are widely spread and in Brazil, the Bothrops moojeni is a medically important species. The pharmacological effects of bothropic snake venoms include pain, blisters, bleeding, necrosis and even amputation of the affected limb. Snake venom metalloproteinases are enzymes abundantly present in venom from Bothrops snakes. These enzymes can cause hemorrhagic effects and lead to myonecrosis due to ischemia. Here, we present BmooMP-I, a new P-I class of metalloproteinase (this class only has the catalytic domain in the mature form) isolated from B. moojeni venom. This protein is able to express fibrinogenolytic and gelatinase activities, which play important roles in the prey's immobilization and digestion, and also induces weak hemorrhagic effect. The primary sequence assignment was done by a novel method, SEQUENCE SLIDER, which combines crystallographic, bioinformatics and mass spectrometry data. The high-resolution crystal structure reveals the monomeric assembly and the conserved metal binding site HExxHxxGxxH with the natural substitution Gly148Asp that does not interfere in the zinc coordination. The presence of a structural calcium ion on the surface of the protein, which can play an important role in the stabilization of hemorrhagic toxins, was observed in the BmooMP-I structure. Due to the relevant local and systemic effects of snake venom metalloproteinases, studies involving these proteins help to better understand the pathological effects of snakebite envenoming.

PubMed: 32946987
DOI: 10.1016/j.biochi.2020.09.001

実験手法

X-RAY DIFFRACTION (1.92 Å)