Crystal structures of Enoyl-ACP reductases I (FabI) and III (FabL) from B. subtilis |
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Authors: | Kim Kook-Han Ha Byung Hak Kim Su Jin Hong Seung Kon Hwang Kwang Yeon Kim Eunice Eunkyeong |
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Institution: | 1 Life Sciences Division, Korea Institute of Science and Technology, 39-1 Hawolkok-dong, Sungbuk-gu, Seoul 136-791, South Korea2 Division of Biotechnology, College of Life Sciences and Biotechnology, Korea University, Seoul 136-701, South Korea |
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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. |
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Keywords: | fatty acid biosynthesis enoyl-ACP reductase FabI FabL crystal structure |
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