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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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:
Online Access:https://www.mdpi.com/2073-4352/9/9/471
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spelling doaj-9dbf3d1b8cec4a31bace40249b15d7042020-11-25T02:01:12ZengMDPI AGCrystals2073-43522019-09-019947110.3390/cryst9090471cryst9090471Crystal Structure of NADPH-Dependent Methylglyoxal Reductase Gre2 from <i>Candida Albicans</i>Giang Thu Nguyen0Shinae Kim1Hyeonseok Jin2Dong-Hyung Cho3Hang-Suk Chun4Woo-Keun Kim5Jeong Ho Chang6Department of Biology Education, Kyungpook National University, Daegu 41566, KoreaDepartment of Biology Education, Kyungpook National University, Daegu 41566, KoreaResearch Institute for Phylogenomics and Evolution, Kyungpook National University, Daegu 41566, KoreaSchool of Life Sciences, Kyungpook National University, Daegu 41566, KoreaBiosystem Research Group, Korea Institute of Toxicology, Daejeon 34114, KoreaBiosystem Research Group, Korea Institute of Toxicology, Daejeon 34114, KoreaDepartment of Biology Education, Kyungpook National University, Daegu 41566, KoreaGre2 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.https://www.mdpi.com/2073-4352/9/9/471Gre2methylglyoxal reductaseNADPHSDR family<i>Candida albicans</i>
collection DOAJ
language English
format Article
sources DOAJ
author Giang Thu Nguyen
Shinae Kim
Hyeonseok Jin
Dong-Hyung Cho
Hang-Suk Chun
Woo-Keun Kim
Jeong Ho Chang
spellingShingle Giang Thu Nguyen
Shinae Kim
Hyeonseok Jin
Dong-Hyung Cho
Hang-Suk Chun
Woo-Keun Kim
Jeong Ho Chang
Crystal Structure of NADPH-Dependent Methylglyoxal Reductase Gre2 from <i>Candida Albicans</i>
Crystals
Gre2
methylglyoxal reductase
NADPH
SDR family
<i>Candida albicans</i>
author_facet Giang Thu Nguyen
Shinae Kim
Hyeonseok Jin
Dong-Hyung Cho
Hang-Suk Chun
Woo-Keun Kim
Jeong Ho Chang
author_sort Giang Thu Nguyen
title Crystal Structure of NADPH-Dependent Methylglyoxal Reductase Gre2 from <i>Candida Albicans</i>
title_short Crystal Structure of NADPH-Dependent Methylglyoxal Reductase Gre2 from <i>Candida Albicans</i>
title_full Crystal Structure of NADPH-Dependent Methylglyoxal Reductase Gre2 from <i>Candida Albicans</i>
title_fullStr Crystal Structure of NADPH-Dependent Methylglyoxal Reductase Gre2 from <i>Candida Albicans</i>
title_full_unstemmed Crystal Structure of NADPH-Dependent Methylglyoxal Reductase Gre2 from <i>Candida Albicans</i>
title_sort crystal structure of nadph-dependent methylglyoxal reductase gre2 from <i>candida albicans</i>
publisher MDPI AG
series Crystals
issn 2073-4352
publishDate 2019-09-01
description 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.
topic Gre2
methylglyoxal reductase
NADPH
SDR family
<i>Candida albicans</i>
url https://www.mdpi.com/2073-4352/9/9/471
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