Crystal structures of Enoyl-ACP reductases I (FabI) and III (FabL) from B. subtilis

Title
Crystal structures of Enoyl-ACP reductases I (FabI) and III (FabL) from B. subtilis
Authors
김국한하병학김수진홍승곤황광연김은경
Keywords
fatty acid biosynthesis; enoyl-ACP reductase; FabI; FabL; crystal structure
Issue Date
2011-02
Publisher
Journal of molecular biology
Citation
VOL 406, NO 3, 403-415
Abstract
Enoyl-[acyl carrier protein] (ACP) reductase (ENR) is a key enzyme in type II fatty acid synthesis that catalyzes the last step in each elongation cycle. Therefore, it has been considered as a target for antibiotics. However, recent studies indicate that some pathogens have more than one ENR; in particular, Bacillus subtilis has two ENRs, FabI and FabL. The crystal structures of the ternary complexes of BsFaBI and BsFabL are found as a homotetramer showing the same overall structure despite a sequence identity of only 24%. The positions of the catalytic dyad of Tyr-(Xaa)6-Lys in FabL are almost identical to that of FabI, but a detailed structural analysis shows that FabL shares more structural similarities with FabG and other members of the SDR (short-chain alcohol dehydrogenase/reductase) family. The apo FabL structure shows significantly different conformations at the cofactor and the substrate-binding regions, and this resulted in a totally different tetrameric arrangement reflecting the flexibility of these regions in the absence of the cofactor and substrate/inhibitor.
URI
http://pubs.kist.re.kr/handle/201004/41793
ISSN
0022-2836
Appears in Collections:
KIST Publication > Article
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