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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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 Å, 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 α12 and β3′ 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 Å, 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 α12 and β3′ 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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