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

38 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

Bibliographical note

Funding Information:
We thank Drs. Jin Ho Moon, Kyung Hwa Kim and Kyung Jin Kim for assistance in data collection. This work was supported financially by the Functional Proteomics Center, the 21C Frontier Research & Development Program of the Korea Ministry of Science and Technology and a Korea Institute of Science and Technology grant.


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

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology


Dive into the research topics of 'Crystal structures of enoyl-ACP reductases i (FabI) and III (FabL) from B. subtilis'. Together they form a unique fingerprint.

Cite this