1GOY
HYDROLASE(ENDORIBONUCLEASE)RIBONUCLEASE BI(G SPECIFIC ENDONUCLEASE) (E.C.3.1.27.-) COMPLEXED WITH GUANOSINE-3'-PHOSPHATE (3'-GMP)
1GOY の概要
エントリーDOI | 10.2210/pdb1goy/pdb |
関連するPDBエントリー | 1BUJ 1GOU 1GOV 2RBI |
分子名称 | RIBONUCLEASE, GUANOSINE-3'-MONOPHOSPHATE, SULFATE ION, ... (4 entities in total) |
機能のキーワード | hydrolase, endoribonuclease, nuclease |
由来する生物種 | BACILLUS INTERMEDIUS |
細胞内の位置 | Secreted: P00649 |
タンパク質・核酸の鎖数 | 2 |
化学式量合計 | 26600.39 |
構造登録者 | Polyakov, K.M.,Lebedev, A.A.,Pavlovsky, A.G.,Sanishvili, R.G.,Dodson, G.G. (登録日: 2001-10-26, 公開日: 2001-11-29, 最終更新日: 2024-05-08) |
主引用文献 | Polyakov, K.M.,Lebedev, A.A.,Okorokov, A.L.,Panov, K.I.,Schulga, A.A.,Pavlovsky, A.G.,Karpeisky, M.Y.A.,Dodson, G.G. The Structure of Substrate-Free Microbial Ribonuclease Binase and of its Complexes with 3'Gmp and Sulfate Ions Acta Crystallogr.,Sect.D, 58:744-, 2002 Cited by PubMed Abstract: The structures of Bacillus intermedius ribonuclease (binase), an extracellular 109-residue enzyme, and its complexes with 3'GMP and sulfate ions were solved at 1.65 and 2.0 A, respectively. The structures were refined using REFMAC. The crystal of free binase belongs to the space group C2, whereas the crystals of complexes belong to the space group P2(1)2(1)2(1). In both crystal lattices the asymmetric unit contains two molecules which form an identical dimer. The structure of the dimer is such that only one of its subunits can bind the nucleotide in the 3'GMP-binase complex, where the guanyl base is located in the recognition loop of the enzyme. In both binase complex structures the phosphate group of 3'GMP or one of the sulfate ions make an electrostatic interaction with the binase molecule at the catalytic site. A second phosphate-binding site was found in the structures of the complexes at the cleft formed by the loop 34-39, the main chain of Arg82 and the side chain of Trp34. Comparison of the complex and unliganded enzyme crystal structures shows that there are some small but distinct differences in the specificity loop (56-62) and in the loops 34-39 and 99-104 associated with the binding of the nucleotide and sulfate ions. PubMed: 11976484DOI: 10.1107/S0907444902003207 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2 Å) |
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