1q7c
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(New page: 200px<br /><applet load="1q7c" size="450" color="white" frame="true" align="right" spinBox="true" caption="1q7c, resolution 2.50Å" /> '''The structure of bet...)
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Revision as of 22:19, 20 November 2007
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The structure of betaketoacyl-[ACP] reductase Y151F mutant in complex with NADPH fragment
Overview
beta-Ketoacyl-acyl carrier protein reductase (FabG) is a key component in, the type II fatty acid synthase system. The structures of Escherichia coli, FabG and the FabG[Y151F] mutant in binary complexes with NADP(H) reveal, that mechanistically important conformational changes accompany cofactor, binding. The active site Ser-Tyr-Lys triad is repositioned into a, catalytically competent constellation, and a hydrogen bonded network, consisting of ribose hydroxyls, the Ser-Tyr-Lys triad, and four water, molecules creates a proton wire to replenish the tyrosine proton donated, during catalysis. Also, a disordered loop in FabG forms a substructure in, the complex that shapes the entrance to the active site. A key observation, is that the nicotinamide portion of the cofactor is disordered in the, FabG[Y151F].NADP(H) complex, and Tyr151 appears to be necessary for, high-affinity cofactor binding. Biochemical data confirm that FabG[Y151F], is defective in NADPH binding. Finally, structural changes consistent with, the observed negative cooperativity of FabG are described.
About this Structure
1Q7C is a Single protein structure of sequence from Escherichia coli with NAP as ligand. Active as [acyl-carrier-protein_reductase 3-oxoacyl-[acyl-carrier-protein] reductase], with EC number 1.1.1.100 Full crystallographic information is available from OCA.
Reference
Cofactor-induced conformational rearrangements establish a catalytically competent active site and a proton relay conduit in FabG., Price AC, Zhang YM, Rock CO, White SW, Structure. 2004 Mar;12(3):417-28. PMID:15016358 [[Category: 3-oxoacyl-[acyl-carrier-protein] reductase]]
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