1HYF
RIBONUCLEASE T1 V16A MUTANT IN COMPLEX WITH SR2+
1HYF の概要
エントリーDOI | 10.2210/pdb1hyf/pdb |
分子名称 | GUANYL-SPECIFIC RIBONUCLEASE T1, STRONTIUM ION, GUANOSINE-2'-MONOPHOSPHATE, ... (4 entities in total) |
機能のキーワード | ribonuclease, stability, metal binding, hydrolase |
由来する生物種 | Aspergillus oryzae |
タンパク質・核酸の鎖数 | 1 |
化学式量合計 | 11517.48 |
構造登録者 | De Swarte, J.,De Vos, S.,Langhorst, U.,Steyaert, J.,Loris, R. (登録日: 2001-01-19, 公開日: 2001-02-14, 最終更新日: 2024-10-09) |
主引用文献 | Deswarte, J.,De Vos, S.,Langhorst, U.,Steyaert, J.,Loris, R. The contribution of metal ions to the conformational stability of ribonuclease T1: crystal versus solution. Eur.J.Biochem., 268:3993-4000, 2001 Cited by PubMed Abstract: In the crystalline state, ribonuclease T1 binds calcium ions at different lattice-dependent positions. In solution, its conformational stability is also remarkably increased in the presence of divalent metal ions. Combining urea unfolding studies and X-ray crystallography, we compared the presence of several metal ions at specific sites in the protein to their contribution to the overall stabilizing effect in solution. We constructed thermodynamic cycles involving particular metal ions and specific carboxylate functions. The resulting coupling energies indicate that some (but not all) metal ions found at lattice contacts in crystal structures may indeed significantly contribute to stability enhancement in the presence of metal ions in solution. PubMed: 11453993DOI: 10.1046/j.1432-1327.2001.02310.x 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (1.7 Å) |
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