5mgb | pdb_00005mgb

Crystal Structure of Rat Peroxisomal Multifunctional enzyme Type-1 (RPMFE1) Complexed with Acetoacetyl-CoA and NAD

spinqualitylabelsall models 5mgb, resolution 2.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5mgb is a 2 chain structure with sequence from Rattus norvegicus. This structure supersedes the now removed PDB entry 5aak. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.8Å Ligands: CAA, GOL, NAD, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function ECHP_RAT Publication Abstract from PubMed Multifunctional enzyme, type-1 (MFE1) is a monomeric enzyme with a 2E-enoyl-CoA hydratase and a 3S-hydroxyacyl-CoA dehydrogenase (HAD) active site. Enzyme kinetic data of rat peroxisomal MFE1 show that the catalytic efficiencies for converting the short-chain substrate 2E-butenoyl-CoA into acetoacetyl-CoA are much lower when compared with those of the homologous monofunctional enzymes. The mode of binding of acetoacetyl-CoA (to the hydratase active site) and the very similar mode of binding of NAD (+) and NADH (to the HAD part) are described and compared with those of their monofunctional counterparts. Structural comparisons suggest that the conformational flexibility of the HAD and hydratase parts of MFE1 are correlated. The possible importance of the conformational flexibility of MFE1 for its biocatalytic properties is discussed. Database: Structural data are available in PDB database under the accession number 5MGB. Structural enzymology comparisons of multifunctional enzyme, type-1 (MFE1): the flexibility of its dehydrogenase part.,Kasaragod P, Midekessa GB, Sridhar S, Schmitz W, Kiema TR, Hiltunen JK, Wierenga RK FEBS Open Bio. 2017 Nov 6;7(12):1830-1842. doi: 10.1002/2211-5463.12337., eCollection 2017 Dec. PMID:29226071 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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