3JU5
Crystal Structure of Dimeric Arginine Kinase at 1.75-A Resolution
Summary for 3JU5
| Entry DOI | 10.2210/pdb3ju5/pdb |
| Related | 3JU6 |
| Descriptor | Arginine kinase, MAGNESIUM ION (3 entities in total) |
| Functional Keywords | arginine kinase, reciprocating mechanism, negative cooperativity, phosphagen kinase, atp-binding, kinase, nucleotide-binding, transferase |
| Biological source | Apostichopus japonicus (Sea cucumber) |
| Total number of polymer chains | 4 |
| Total formula weight | 171138.35 |
| Authors | |
| Primary citation | Wu, X.,Ye, S.,Guo, S.,Yan, W.,Bartlam, M.,Rao, Z. Structural basis for a reciprocating mechanism of negative cooperativity in dimeric phosphagen kinase activity Faseb J., 24:242-252, 2010 Cited by PubMed Abstract: 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. PubMed: 19783784DOI: 10.1096/fj.09-140194 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.75 Å) |
Structure validation
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