3JU6
Crystal Structure of Dimeric Arginine Kinase in Complex with AMPPNP and Arginine
3JU6 の概要
| エントリーDOI | 10.2210/pdb3ju6/pdb |
| 関連するPDBエントリー | 3JU5 |
| 分子名称 | Arginine kinase, ARGININE, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, ... (4 entities in total) |
| 機能のキーワード | arginine kinase, reciprocating mechanism, negative cooperativity, phosphagen kinase, ternary complex, atp-binding, kinase, nucleotide-binding, transferase |
| 由来する生物種 | Apostichopus japonicus (Sea cucumber) |
| タンパク質・核酸の鎖数 | 4 |
| 化学式量合計 | 171771.14 |
| 構造登録者 | |
| 主引用文献 | 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 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.45 Å) |
構造検証レポート
検証レポート(詳細版)
をダウンロード






