Kim, Kook-Han Ha, Byung Hak Kim, Su Jin Hong, Seung Kon Hwang, Kwang Yeon Kim, Eunice EunKyeong 2024-01-20T17:33:10Z 2024-01-20T17:33:10Z 2021-09-02 2011-02-25 0022-2836 https://pubs.kist.re.kr/handle/201004/130629 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. English ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD ACYL CARRIER PROTEIN X-RAY-STRUCTURE SUBSTRATE-BINDING TRICLOSAN INHIBITION TARGET MECHANISM INHA BIOSYNTHESIS RESISTANT Crystal Structures of Enoyl-ACP Reductases I (FabI) and III (FabL) from B. subtilis Article 10.1016/j.jmb.2010.12.003 1 JOURNAL OF MOLECULAR BIOLOGY, v.406, no.3, pp.403 - 415 JOURNAL OF MOLECULAR BIOLOGY 406 3 403 415 scie scopus 000287831500005 2-s2.0-79551681011 Biochemistry & Molecular Biology Biochemistry & Molecular Biology Article ACYL CARRIER PROTEIN X-RAY-STRUCTURE SUBSTRATE-BINDING TRICLOSAN INHIBITION TARGET MECHANISM INHA BIOSYNTHESIS RESISTANT fatty acid biosynthesis enoyl-ACP reductase FabI FabL crystal structure