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- W2000956496 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." @default.
- W2000956496 created "2016-06-24" @default.
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- W2000956496 date "2011-02-01" @default.
- W2000956496 modified "2023-10-18" @default.
- W2000956496 title "Crystal Structures of Enoyl-ACP Reductases I (FabI) and III (FabL) from B. subtilis" @default.
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- W2000956496 doi "https://doi.org/10.1016/j.jmb.2010.12.003" @default.
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