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Open AccessArticle

Crystal Structure of the Active Site Mutant Form of Soluble Fumarate Reductase, Osm1

College of Pharmacy, Chung-Ang University, Seoul 06974, Korea
Author to whom correspondence should be addressed.
These authors are contributed equally to this work.
Crystals 2019, 9(10), 504;
Received: 15 September 2019 / Revised: 25 September 2019 / Accepted: 27 September 2019 / Published: 27 September 2019
(This article belongs to the Special Issue Crystallographic Studies of Enzymes)
Soluble fumarate reductase is essential for survival under anaerobic conditions. This enzyme can maintain the redox balance in the cell by catalyzing the reduction of fumarate to succinate. Although the overall reaction mechanism of soluble fumarate reductase in yeast, Osm1, has been proposed by a previous structural study, the details of the underlying mechanism are not completely elucidated. The present study provides the structural information regarding the active site mutant form of Osm1 (R326A), thus, revealing that R326A mutation does not affect the substrate binding. Structural alterations of the residues surrounding the active site, and the missing 2nd flavin adenine dinucleotide (FAD) in the previously defined 2nd FAD binding site, were observed as characteristic features of the Osm1 R326A crystal structure. Based on these findings, we provided a clue that can explain the loss of activity of Osm1 R326A. View Full-Text
Keywords: anaerobiosis; soluble fumarate reductase; crystal structure anaerobiosis; soluble fumarate reductase; crystal structure
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Kim, C.M.; Kwon, S.; Jung, K.H.; Chun, H.L.; Ha, H.J.; Park, H.H. Crystal Structure of the Active Site Mutant Form of Soluble Fumarate Reductase, Osm1. Crystals 2019, 9, 504.

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