1i01 | pdb_00001i01

CRYSTAL STRUCTURE OF BETA-KETOACYL [ACYL CARRIER PROTEIN] REDUCTASE FROM E. COLI.

spinqualitylabelsall models 1i01, resolution 2.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1i01 is a 8 chain structure with sequence from Escherichia coli. The June 2007 RCSB PDB Molecule of the Month feature on Fatty Acid Synthase by David S. Goodsell is 10.2210/rcsb_pdb/mom_2007_6. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Activity: [acyl-carrier-protein_reductase 3-oxoacyl-[acyl-carrier-protein] reductase], with EC number 1.1.1.100 Resources: FirstGlance, OCA, RCSB, PDBsum 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 PubMed The structure of beta-ketoacyl-[acyl carrier protein] reductase (FabG) from Escherichia coli was determined via the multiwavelength anomalous diffraction technique using a selenomethionine-labeled crystal containing 88 selenium sites in the asymmetric unit. The comparison of the E. coli FabG structure with the homologous Brassica napus FabG.NADP(+) binary complex reveals that cofactor binding causes a substantial conformational change in the protein. This conformational change puts all three active-site residues (Ser 138, Tyr 151, and Lys 155) into their active configurations and provides a structural mechanism for allosteric communication between the active sites in the homotetramer. FabG exhibits negative cooperative binding of NADPH, and this effect is enhanced by the presence of acyl carrier protein (ACP). NADPH binding also increases the affinity and decreases the maximum binding of ACP to FabG. Thus, unlike other members of the short-chain dehydrogenase/reductase superfamily, FabG undergoes a substantial conformational change upon cofactor binding that organizes the active-site triad and alters the affinity of the other substrate-binding sites in the tetrameric enzyme. Structure of beta-ketoacyl-[acyl carrier protein] reductase from Escherichia coli: negative cooperativity and its structural basis.,Price AC, Zhang YM, Rock CO, White SW Biochemistry. 2001 Oct 30;40(43):12772-81. PMID:11669613 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Beta-ketoacyl-ACP reductase

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