3dt4

The structure of rat cytosolic PEPCK in complex with oxalate and GTP

spinqualitylabelsall models 3dt4, resolution 1.45Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3dt4 is a 2 chain structure with sequence from Rattus norvegicus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: 1PE, GTP, MN, NA, OXL Related: 3dt2, 3dt7, 3dtb Gene: Pck1 (Rattus norvegicus) Activity: Phosphoenolpyruvate carboxykinase (GTP), with EC number 4.1.1.32 Resources: FirstGlance, OCA, RCSB, PDBsum Function [PPCKC_RAT] Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP), the rate-limiting step in the metabolic pathway that produces glucose from lactate and other precursors derived from the citric acid cycle. 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 induced fit and conformational selection/population shift models are two extreme cases of a continuum aimed at understanding the mechanism by which the final key-lock or active enzyme conformation is achieved upon formation of the correctly ligated enzyme. Structures of complexes representing the Michaelis and enolate intermediate complexes of the reaction catalyzed by phosphoenolpyruvate carboxykinase provide direct structural evidence for the encounter complex that is intrinsic to the induced fit model and not required by the conformational selection model. In addition, the structural data demonstrate that the conformational selection model is not sufficient to explain the correlation between dynamics and catalysis in phosphoenolpyruvate carboxykinase and other enzymes in which the transition between the uninduced and the induced conformations occludes the active site from the solvent. The structural data are consistent with a model in that the energy input from substrate association results in changes in the free energy landscape for the protein, allowing for structural transitions along an induced fit pathway. Enzymes with lid-gated active sites must operate by an induced fit mechanism instead of conformational selection.,Sullivan SM, Holyoak T Proc Natl Acad Sci U S A. 2008 Sep 16;105(37):13829-34. Epub 2008 Sep 4. PMID:18772387 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Phosphoenolpyruvate carboxykinase

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