Crystal Structure of the Active Site Mutant Form of Soluble Fumarate Reductase, Osm1
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 p...
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doaj-3fd6e05a29e04c6b911874bf31cd60f92020-11-25T02:13:43ZengMDPI AGCrystals2073-43522019-09-0191050410.3390/cryst9100504cryst9100504Crystal Structure of the Active Site Mutant Form of Soluble Fumarate Reductase, Osm1Chang Min Kim0Sunghark Kwon1Kyung Ho Jung2Hye Lin Chun3Hyun Ji Ha4Hyun Ho Park5College of Pharmacy, Chung-Ang University, Seoul 06974, KoreaCollege of Pharmacy, Chung-Ang University, Seoul 06974, KoreaCollege of Pharmacy, Chung-Ang University, Seoul 06974, KoreaCollege of Pharmacy, Chung-Ang University, Seoul 06974, KoreaCollege of Pharmacy, Chung-Ang University, Seoul 06974, KoreaCollege of Pharmacy, Chung-Ang University, Seoul 06974, KoreaSoluble 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.https://www.mdpi.com/2073-4352/9/10/504anaerobiosissoluble fumarate reductasecrystal structure |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Chang Min Kim Sunghark Kwon Kyung Ho Jung Hye Lin Chun Hyun Ji Ha Hyun Ho Park |
spellingShingle |
Chang Min Kim Sunghark Kwon Kyung Ho Jung Hye Lin Chun Hyun Ji Ha Hyun Ho Park Crystal Structure of the Active Site Mutant Form of Soluble Fumarate Reductase, Osm1 Crystals anaerobiosis soluble fumarate reductase crystal structure |
author_facet |
Chang Min Kim Sunghark Kwon Kyung Ho Jung Hye Lin Chun Hyun Ji Ha Hyun Ho Park |
author_sort |
Chang Min Kim |
title |
Crystal Structure of the Active Site Mutant Form of Soluble Fumarate Reductase, Osm1 |
title_short |
Crystal Structure of the Active Site Mutant Form of Soluble Fumarate Reductase, Osm1 |
title_full |
Crystal Structure of the Active Site Mutant Form of Soluble Fumarate Reductase, Osm1 |
title_fullStr |
Crystal Structure of the Active Site Mutant Form of Soluble Fumarate Reductase, Osm1 |
title_full_unstemmed |
Crystal Structure of the Active Site Mutant Form of Soluble Fumarate Reductase, Osm1 |
title_sort |
crystal structure of the active site mutant form of soluble fumarate reductase, osm1 |
publisher |
MDPI AG |
series |
Crystals |
issn |
2073-4352 |
publishDate |
2019-09-01 |
description |
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. |
topic |
anaerobiosis soluble fumarate reductase crystal structure |
url |
https://www.mdpi.com/2073-4352/9/10/504 |
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