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Crystal Structure of NADPH-Dependent Methylglyoxal Reductase Gre2 from Candida Albicans

1
Department of Biology Education, Kyungpook National University, Daegu 41566, Korea
2
Research Institute for Phylogenomics and Evolution, Kyungpook National University, Daegu 41566, Korea
3
School of Life Sciences, Kyungpook National University, Daegu 41566, Korea
4
Biosystem Research Group, Korea Institute of Toxicology, Daejeon 34114, Korea
*
Authors to whom correspondence should be addressed.
Crystals 2019, 9(9), 471; https://doi.org/10.3390/cryst9090471
Received: 16 August 2019 / Revised: 7 September 2019 / Accepted: 8 September 2019 / Published: 10 September 2019
(This article belongs to the Special Issue Crystallographic Studies of Enzymes)
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 Candida albicans (CaGre2) for both the apo-form and NADPH-complexed form at resolutions of 2.8 and 3.02 Å, respectively. The CaGre2 structure is composed of two distinct domains: the N-terminal cofactor-binding domain and the C-terminal substrate-binding domain. Extensive comparison of CaGre2 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. View Full-Text
Keywords: Gre2; methylglyoxal reductase; NADPH; SDR family; Candida albicans Gre2; methylglyoxal reductase; NADPH; SDR family; Candida albicans
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MDPI and ACS Style

Nguyen, G.T.; Kim, S.; Jin, H.; Cho, D.-H.; Chun, H.-S.; Kim, W.-K.; Chang, J.H. Crystal Structure of NADPH-Dependent Methylglyoxal Reductase Gre2 from Candida Albicans. Crystals 2019, 9, 471.

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