3ju5 | pdb_00003ju5

Crystal Structure of Dimeric Arginine Kinase at 1.75-A Resolution

spinqualitylabelsall models 3ju5, resolution 1.75Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3ju5 is a 4 chain structure with sequence from Apostichopus japonicus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.75Å Ligands: MG, MSE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function KARG_STIJA 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 Phosphagen kinase (PK) family members catalyze the reversible phosphoryl transfer between phosphagen and ADP to reserve or release energy in cell energy metabolism. The structures of classic quaternary complexes of dimeric creatine kinase (CK) revealed asymmetric ligand binding states of two protomers, but the significance and mechanism remain unclear. To understand this negative cooperativity further, we determined the first structure of dimeric arginine kinase (dAK), another PK family member, at 1.75 A, as well as the structure of its ternary complex with AMPPNP and arginine. Further structural analysis shows that the ligand-free protomer in a ligand-bound dimer opens more widely than the protomers in a ligand-free dimer, which leads to three different states of a dAK protomer. The unexpected allostery of the ligand-free protomer in a ligand-bound dimer should be relayed from the ligand-binding-induced allostery of its adjacent protomer. Mutations that weaken the interprotomer connections dramatically reduced the catalytic activities of dAK, indicating the importance of the allosteric propagation mediated by the homodimer interface. These results suggest a reciprocating mechanism of dimeric PK, which is shared by other ATP related oligomeric enzymes, e.g., ATP synthase. Structural basis for a reciprocating mechanism of negative cooperativity in dimeric phosphagen kinase activity.,Wu X, Ye S, Guo S, Yan W, Bartlam M, Rao Z FASEB J. 2010 Jan;24(1):242-52. Epub 2009 Sep 25. PMID:19783784 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Arginine kinase 3D structures

Proteopedia Page Contributors and Editors (what is this?)

OCA