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Structural insights into cofactor recognition of yeast mitochondria 3-oxoacyl-ACP reductase OAR1.
MedLine Citation:
PMID:  23300157     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
3-Oxoacyl-(acyl-carrier-protein) reductase (OAR1 or FabG, EC.1.1.1.100) is responsible for the first reductive step in fatty acid biosynthesis using Nicotinamide Adenine Dinucleotide Phosphate (NADPH) as a cofactor. Recent studies suggest there is a fatty acid synthetase II pathway that consists of a series of separate enzymes in yeast mitochondrion. Here, we present the crystal structure of the yeast mitochondria OAR1 (ymtOAR1) alone in apo-form at 2.60 Å and complexed with NADPH at 2.10 Å resolution. Unlike the reported tetrameric OARs, ymtOAR1 forms a homodimer due to the different fold. The enzyme generates conformational changes upon NADPH binding to the active site. Moreover, two different cofactor-binding patterns are observed from two forms of complex crystals, and structural analysis implies the adenine end of cofactor may recognize enzyme prior to nicotinaminde end. Additionally, biochemical studies suggest Arg14 is important for cofactor recognition of ymtOAR1. © 2013 IUBMB Life, 2013.
Authors:
Yujie Zhang; Fangkun Ning; Xu Li; Maikun Teng
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2013-1-9
Journal Detail:
Title:  IUBMB life     Volume:  -     ISSN:  1521-6551     ISO Abbreviation:  IUBMB Life     Publication Date:  2013 Jan 
Date Detail:
Created Date:  2013-1-9     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  100888706     Medline TA:  IUBMB Life     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Copyright Information:
Copyright © 2013 International Union of Biochemistry and Molecular Biology, Inc.
Affiliation:
Hefei National Laboratory for Physical Sciences at the Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, Anhui, China; Key Laboratory of Structural Biology, Chinese Academy of Sciences, Hefei, Anhui, China.
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