1wdk | pdb_00001wdk

fatty acid beta-oxidation multienzyme complex from Pseudomonas fragi, form I (native2)

spinqualitylabelsall models 1wdk, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1wdk is a 4 chain structure with sequence from "bacterium_fragi"_eichholz_1902 "bacterium fragi" eichholz 1902. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ACO, HG, N8E, NAD, ZN Related: 1wdl, 1wdm Activity: Acetyl-CoA C-acyltransferase, with EC number 2.3.1.16 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [FADB_PSEFR] Involved in the aerobic and anaerobic degradation of long-chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate.[HAMAP-Rule:MF_01621] 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 atomic view of the active site coupling termed channelling is a major subject in molecular biology. We have determined two distinct crystal structures of the bacterial multienzyme complex that catalyzes the last three sequential reactions in the fatty acid beta-oxidation cycle. The alpha2beta2 heterotetrameric structure shows the uneven ring architecture, where all the catalytic centers of 2-enoyl-CoA hydratase (ECH), L-3-hydroxyacyl-CoA dehydrogenase (HACD) and 3-ketoacyl-CoA thiolase (KACT) face a large inner solvent region. The substrate, anchored through the 3'-phosphate ADP moiety, allows the fatty acid tail to pivot from the ECH to HACD active sites, and finally to the KACT active site. Coupling with striking domain rearrangements, the incorporation of the tail into the KACT cavity and the relocation of 3'-phosphate ADP bring the reactive C2-C3 bond to the correct position for cleavage. The alpha-helical linker specific for the multienzyme contributes to the pivoting center formation and the substrate transfer through its deformation. This channelling mechanism could be applied to other beta-oxidation multienzymes, as revealed from the homology model of the human mitochondrial trifunctional enzyme complex. Structural basis for channelling mechanism of a fatty acid beta-oxidation multienzyme complex.,Ishikawa M, Tsuchiya D, Oyama T, Tsunaka Y, Morikawa K EMBO J. 2004 Jul 21;23(14):2745-54. Epub 2004 Jul 1. PMID:15229654 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Thiolase

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