4E0V

Structure of L-amino acid oxidase from the B. jararacussu venom

4E0V の概要

• エントリーDOI: 10.2210/pdb4e0v/pdb
• 分子名称: L-amino-acid oxidase, FLAVIN-ADENINE DINUCLEOTIDE (3 entities in total)
• 機能のキーワード: l-amino acid oxidase, fad-binding mode, oxidoreductase
• 由来する生物種: Bothrops jararacussu (Jararacussu)
• 細胞内の位置: Secreted (By similarity): Q6TGQ9
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 114288.01

構造登録者

Ullah, A.,Souza, T.A.C.B.,Betzel, C.,Murakami, M.T.,Arni, R.K. (登録日: 2012-03-05, 公開日: 2012-04-25, 最終更新日: 2024-11-27)

主引用文献

Ullah, A.,Souza, T.A.,Abrego, J.R.,Betzel, C.,Murakami, M.T.,Arni, R.K.
Structural insights into selectivity and cofactor binding in snake venom L-amino acid oxidases.
Biochem.Biophys.Res.Commun., 421:124-128, 2012

PubMed Abstract: L-Amino acid oxidases (LAAOs) are flavoenzymes that catalytically deaminate L-amino acids to corresponding α-keto acids with the concomitant production of ammonia (NH(3)) and hydrogen peroxide (H(2)O(2)). Particularly, snake venom LAAOs have been attracted much attention due to their diverse clinical and biological effects, interfering on human coagulation factors and being cytotoxic against some pathogenic bacteria and Leishmania ssp. In this work, a new LAAO from Bothrops jararacussu venom (BjsuLAAO) was purified, functionally characterized and its structure determined by X-ray crystallography at 3.1 Å resolution. BjsuLAAO showed high catalytic specificity for aromatic and aliphatic large side-chain amino acids. Comparative structural analysis with prokaryotic LAAOs, which exhibit low specificity, indicates the importance of the active-site volume in modulating enzyme selectivity. Surprisingly, the flavin adenine dinucleotide (FAD) cofactor was found in a different orientation canonically described for both prokaryotic and eukaryotic LAAOs. In this new conformational state, the adenosyl group is flipped towards the 62-71 loop, being stabilized by several hydrogen-bond interactions, which is equally stable to the classical binding mode.

PubMed: 22490662
DOI: 10.1016/j.bbrc.2012.03.129

実験手法

X-RAY DIFFRACTION (3.1 Å)