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.
journal_name
J Mol Bioljournal_title
Journal of molecular biologyauthors
Kim KH,Ha BH,Kim SJ,Hong SK,Hwang KY,Kim EEdoi
10.1016/j.jmb.2010.12.003subject
Has Abstractpub_date
2011-02-25 00:00:00pages
403-15issue
3eissn
0022-2836issn
1089-8638pii
S0022-2836(10)01291-Xjournal_volume
406pub_type
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