6BNN

Crystal structure of V278E-glyoxalase I mutant from Zea mays in space group P4(1)2(1)2

6BNN の概要

• エントリーDOI: 10.2210/pdb6bnn/pdb
• 関連するPDBエントリー: 5D7Z
• 分子名称: Lactoylglutathione lyase, GLUTATHIONE, COBALT (II) ION, ... (5 entities in total)
• 機能のキーワード: plant protein
• 由来する生物種: Zea mays (Maize)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 33447.70

構造登録者

Alvarez, C.E.,Agostini, R.B.,Gonzalez, J.M.,Drincovich, M.F.,Campos Bermudez, V.A.,Klinke, S. (登録日: 2017-11-17, 公開日: 2018-11-21, 最終更新日: 2023-10-04)

主引用文献

Gonzalez, J.M.,Agostini, R.B.,Alvarez, C.E.,Klinke, S.,Andreo, C.S.,Campos-Bermudez, V.A.
Deciphering the number and location of active sites in the monomeric glyoxalase I of Zea mays.
Febs J., 286:3255-3271, 2019

PubMed Abstract: Detoxification of methylglyoxal, a toxic by-product of central sugar metabolism, is a major issue for all forms of life. The glyoxalase pathway evolved to effectively convert methylglyoxal into d-lactate via a glutathione hemithioacetal intermediate. Recently, we have shown that the monomeric glyoxalase I from maize exhibits a symmetric fold with two cavities, potentially harboring two active sites, in analogy with homodimeric enzyme surrogates. Here we confirm that only one of the two cavities exhibits glyoxalase I activity and show that it adopts a tunnel-shaped structure upon substrate binding. Such conformational change gives rise to independent binding sites for glutathione and methylglyoxal in the same active site, with important implications for the molecular reaction mechanism, which has been a matter of debate for several decades. DATABASE: Structural data are available in The Protein Data Bank database under the accession numbers 6BNN, 6BNX, and 6BNZ.

PubMed: 30993890
DOI: 10.1111/febs.14855

実験手法

X-RAY DIFFRACTION (1.55 Å)