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

Kook Han Kim, Byung Hak Ha, Su Jin Kim, Seung Kon Hong, Kwang Yeon Hwang, Eunice Eunkyeong Kim

Research output: Contribution to journalArticlepeer-review

35 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)403-415
Number of pages13
JournalJournal of Molecular Biology
Issue number3
Publication statusPublished - 2011 Feb 25


  • FabI
  • FabL
  • crystal structure
  • enoyl-ACP reductase
  • fatty acid biosynthesis

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology


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