Crystal Structures of Enoyl-ACP Reductases I (FabI) and III (FabL) from B. subtilis
- Authors
- Kim, Kook-Han; Ha, Byung Hak; Kim, Su Jin; Hong, Seung Kon; Hwang, Kwang Yeon; Kim, Eunice EunKyeong
- Issue Date
- 25-2월-2011
- Publisher
- ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
- Keywords
- fatty acid biosynthesis; enoyl-ACP reductase; FabI; FabL; crystal structure
- Citation
- JOURNAL OF MOLECULAR BIOLOGY, v.406, no.3, pp.403 - 415
- Indexed
- SCIE
SCOPUS
- Journal Title
- JOURNAL OF MOLECULAR BIOLOGY
- Volume
- 406
- Number
- 3
- Start Page
- 403
- End Page
- 415
- URI
- https://scholar.korea.ac.kr/handle/2021.sw.korea/113042
- DOI
- 10.1016/j.jmb.2010.12.003
- ISSN
- 0022-2836
- 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. (C) 2010 Elsevier Ltd. All rights reserved.
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