7r6y

E117K mutant pyruvate kinase from rabbit muscle

spinqualitylabelsall models 7r6y, resolution 2.25Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7r6y is a 4 chain structure with sequence from Oryctolagus cuniculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.25Å Ligands: ACT, MG, OXL Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function KPYM_RABIT Glycolytic enzyme that catalyzes the transfer of a phosphoryl group from phosphoenolpyruvate (PEP) to ADP, generating ATP. Stimulates POU5F1-mediated transcriptional activation (By similarity). Publication Abstract from PubMed Eukarya pyruvate kinases possess glutamate at position 117 (numbering of rabbit muscle enzyme), whereas bacteria have either glutamate or lysine. Those with E117 are K(+)-dependent, whereas those with K117 are K(+)-independent. In a phylogenetic tree, 80% of the sequences with E117 are occupied by T113/K114/T120 and 77% of those with K117 possess L113/Q114/(L,I,V)120. This work aims to understand these residues' contribution to the K(+)-independent pyruvate kinases using the K(+)-dependent rabbit muscle enzyme. Residues 117 and 120 are crucial in the differences between the K(+)-dependent and -independent mutants. K(+)-independent activity increased with L113 and Q114 to K117, but L120 induced structural differences that inactivated the enzyme. T120 appears to be key in folding the protein and closure of the lid of the active site to acquire its active conformation in the K(+)-dependent enzymes. E117K mutant was K(+)-independent and the enzyme acquired the active conformation by a different mechanism. In the K(+)-independent apoenzyme of Mycobacterium tuberculosis, K72 (K117) flips out of the active site; in the holoenzyme, K72 faces toward the active site bridging the substrates through water molecules. The results provide evidence that two different mechanisms have evolved for the catalysis of this reaction. The K(+)-Dependent and -Independent Pyruvate Kinases Acquire the Active Conformation by Different Mechanisms.,Ramirez-Silva L, Hernandez-Alcantara G, Guerrero-Mendiola C, Gonzalez-Andrade M, Rodriguez-Romero A, Rodriguez-Hernandez A, Lugo-Munguia A, Gomez-Coronado PA, Rodriguez-Mendez C, Vega-Segura A Int J Mol Sci. 2022 Jan 25;23(3). pii: ijms23031347. doi: 10.3390/ijms23031347. PMID:35163274 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Pyruvate kinase 3D structures

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