6BNZ

Crystal structure of E144Q-glyoxalase I mutant from Zea mays in space group P4(1)2(1)2

Summary for 6BNZ

• Entry DOI: 10.2210/pdb6bnz/pdb
• Related: 5D7Z 6BNN
• Descriptor: Lactoylglutathione lyase, COBALT (II) ION, GLUTATHIONE, ... (5 entities in total)
• Functional Keywords: plant protein defense, plant protein
• Biological source: Zea mays (Maize)
• Total number of polymer chains: 1
• Total formula weight: 33554.81

Authors

Alvarez, C.E.,Agostini, R.B.,Gonzalez, J.M.,Drincovich, M.F.,Campos Bermudez, V.A.,Klinke, S. (deposition date: 2017-11-17, release date: 2018-11-21, Last modification date: 2023-10-04)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.45 Å)