3e0v | pdb_00003e0v

Crystal structure of pyruvate kinase from Leishmania mexicana in complex with sulphate ions

spinqualitylabelsall models 3e0v, resolution 3.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3e0v is a 6 chain structure with sequence from Leishmania mexicana. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: GOL, SO4 Related: 3e0w Gene: PYK (Leishmania mexicana) Activity: Pyruvate kinase, with EC number 2.7.1.40 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 We report X-ray structures of pyruvate kinase from Leishmania mexicana (LmPYK) that are trapped in different conformations. These, together with the previously reported structure of LmPYK in its inactive (T-state) conformation, allow comparisons of three different conformers of the same species of pyruvate kinase (PYK). Four new site point mutants showing the effects of side-chain alteration at subunit interfaces are also enzymatically characterised. The LmPYK tetramer crystals grown with ammonium sulphate as precipitant adopt an active-like conformation, with sulphate ions at the active and effector sites. The sulphates occupy positions similar to those of the phosphates of ligands bound to active (R-state) and constitutively active (nonallosteric) PYKs from several species, and provide insight into the structural roles of the phosphates of the substrates and effectors. Crystal soaking in sulphate-free buffers was found to induce major conformational changes in the tetramer. In particular, the unwinding of the Aalpha6' helix and the inward hinge movement of the B domain are coupled with a significant widening (4 A) of the tetramer caused by lateral movement of the C domains. The two new LmPYK structures and the activity studies of site point mutations described in this article are consistent with a developing picture of allosteric activity in which localised changes in protein flexibility govern the distribution of conformer families adopted by the tetramer in its active and inactive states. Sulphate removal induces a major conformational change in Leishmania mexicana pyruvate kinase in the crystalline state.,Tulloch LB, Morgan HP, Hannaert V, Michels PA, Fothergill-Gilmore LA, Walkinshaw MD J Mol Biol. 2008 Nov 14;383(3):615-26. Epub 2008 Aug 23. PMID:18775437 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Pyruvate Kinase

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