Crystal Structure of NADPH-Dependent Methylglyoxal Reductase Gre2 from <i>Candida Albicans</i>

Crystal Structure of NADPH-Dependent Methylglyoxal Reductase Gre2 from <i>Candida Albicans</i>

Gre2 is a key enzyme in the methylglyoxal detoxification pathway; it uses NADPH or NADH as an electron donor to reduce the cytotoxic methylglyoxal to lactaldehyde. This enzyme is a member of the short-chain dehydrogenase/reductase (SDR) superfamily whose members catalyze this type of reaction with a...

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Bibliographic Details
Main Authors: Giang Thu Nguyen, Shinae Kim, Hyeonseok Jin, Dong-Hyung Cho, Hang-Suk Chun, Woo-Keun Kim, Jeong Ho Chang
Format: Article
Language:English
Published: MDPI AG 2019-09-01
Series:Crystals
Subjects:
Gre2
methylglyoxal reductase
NADPH
SDR family
<i>Candida albicans</i>
Online Access:https://www.mdpi.com/2073-4352/9/9/471
Description
Summary:Gre2 is a key enzyme in the methylglyoxal detoxification pathway; it uses NADPH or NADH as an electron donor to reduce the cytotoxic methylglyoxal to lactaldehyde. This enzyme is a member of the short-chain dehydrogenase/reductase (SDR) superfamily whose members catalyze this type of reaction with a broad range of substrates. To elucidate the structural features, we determined the crystal structures of the NADPH-dependent methylglyoxal reductase Gre2 from <i>Candida albicans</i> (<i>Ca</i>Gre2) for both the apo-form and NADPH-complexed form at resolutions of 2.8 and 3.02 &#197;, respectively. The <i>Ca</i>Gre2 structure is composed of two distinct domains: the N-terminal cofactor-binding domain and the C-terminal substrate-binding domain. Extensive comparison of <i>Ca</i>Gre2 with its homologous structures reveals conformational changes in &#945;12 and &#946;3&#8242; of the NADPH-complex forms. This study may provide insights into the structural and functional variation of SDR family proteins.
ISSN:2073-4352

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