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Crystal Structure of the Bacillus cereus Enoyl-Acyl Carrier Protein Reductase with NADP+ and indole naphthyridinone (Complex form)Crystal Structure of the Bacillus cereus Enoyl-Acyl Carrier Protein Reductase with NADP+ and indole naphthyridinone (Complex form)
Structural highlights
FunctionFABI_BACCR Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). Involved in the elongation cycle of fatty acid which are used in the lipid metabolism (By similarity). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedEnoyl-[acyl carrier protein] reductase (ENR) is an essential enzyme in type II fatty-acid synthesis that catalyzes the last step in each elongation cycle. Thus far FabI, FabL and FabK have been reported to carry out the reaction, with FabI being the most characterized. Some bacteria have more than one ENR, and Bacillus cereus has two (FabI and FabL) reported. Here, we have determined the crystal structures of the later in the apo form and in the ternary complex with NADP(+) and an indole naphthyridinone inhibitor. The two structures are almost identical, except for the three stretches that are disordered in the apo form. The apo form exists as a homo-dimer in both crystal and solution, while the ternary complex forms a homo-tetramer. The three stretches disordered in the apo structure are important in the cofactor and the inhibitor binding as well as in tetramer formation. Dimeric and tetrameric forms of enoyl-acyl carrier protein reductase from Bacillus cereus.,Kim SJ, Ha BH, Kim KH, Hong SK, Shin KJ, Suh SW, Kim EE Biochem Biophys Res Commun. 2010 Oct 1;400(4):517-22. Epub 2010 Aug 26. PMID:20800575[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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