Dimeric and tetrameric forms of enoyl-acyl carrier protein reductase from Bacillus cereus

Title
Dimeric and tetrameric forms of enoyl-acyl carrier protein reductase from Bacillus cereus
Authors
김수진하병학김국한홍승곤신계정서세원김은경
Keywords
Fatty acid biosynthesis; Enoyl-ACP reductase; Dimer; Tetramer; Crystal structure
Issue Date
2010-10
Publisher
Biochemical and biophysical research communications
Citation
VOL 400, NO 4, 517-522
Abstract
Enoyl-[acyl carrier protein] reductase (ENR) is an essential enzyme in type II fatty-acid synthesis that catalyzes the last step in each elongation cycle. Thus far FabI, FabL and FabK have been reported to carry out the reaction, with FabI being the most characterized. Some bacteria have more than one ENR, and Bacillus cereus has two (FabI and FabL) reported. Here, we have determined the crystal structures of the later in the apo form and in the ternary complex with NADP+ and an indole naphthyridinone inhibitor. The two structures are almost identical, except for the three stretches that are disordered in the apo form. The apo form exists as a homo-dimer in both crystal and solution, while the ternary complex forms a homo-tetramer. The three stretches disordered in the apo structure are important in the cofactor and the inhibitor binding as well as in tetramer formation.
URI
http://pubs.kist.re.kr/handle/201004/38312
ISSN
1090-2104
Appears in Collections:
KIST Publication > Article
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