3hqq | pdb_00003hqq

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Crystal structure of Leishmania mexicana pyruvate kinase (LmPYK) in complex with Fructose 2,6 bisphosphate

spinqualitylabelsall models 3hqq, resolution 5.07Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3hqq is a 24 chain structure with sequence from Leime. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: FDP Related: 3e0v, 3e0w, 1pkl, 3hqn, 3hqo, 3hqp Gene: PYK (LEIME) Activity: Pyruvate kinase, with EC number 2.7.1.40 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Warning: this is a large structure, and loading might take a long time or not happen at all. 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 Allosteric regulation provides a rate management system for enzymes involved in many cellular processes. Ligand-controlled regulation is easily recognizable, but the underlying molecular mechanisms have remained elusive. We have obtained the first complete series of allosteric structures, in all possible ligated states, for the tetrameric enzyme, pyruvate kinase, from Leishmania mexicana. The transition between inactive T-state and active R-state is accompanied by a simple symmetrical 6 degrees rigid body rocking motion of the A- and C-domain cores in each of the four subunits. However, formation of the R-state in this way is only part of the mechanism; eight essential salt bridge locks that form across the C-C interface provide tetramer rigidity with a coupled 7-fold increase in rate. The results presented here illustrate how conformational changes coupled with effector binding correlate with loss of flexibility and increase in thermal stability providing a general mechanism for allosteric control. Allosteric mechanism of pyruvate kinase from Leishmania mexicana uses a rock and lock model.,Morgan HP, McNae IW, Nowicki MW, Hannaert V, Michels PA, Fothergill-Gilmore LA, Walkinshaw MD J Biol Chem. 2010 Apr 23;285(17):12892-8. Epub 2010 Feb 1. PMID:20123988 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Pyruvate Kinase

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