Crystal structures of Enoyl-ACP reductases I (FabI) and III (FabL) from B. subtilis
- Crystal structures of Enoyl-ACP reductases I (FabI) and III (FabL) from B. subtilis
- 김국한; 하병학; 김수진; 홍승곤; 황광연; 김은경
- fatty acid biosynthesis; enoyl-ACP reductase; FabI; FabL; crystal structure
- Issue Date
- Journal of molecular biology
- VOL 406, NO 3, 403-415
- 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.
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