1R5C

X-ray structure of the complex of Bovine seminal ribonuclease swapping dimer with d(CpA)

1R5C の概要

• エントリーDOI: 10.2210/pdb1r5c/pdb
• 関連するPDBエントリー: 1R5D
• 分子名称: Ribonuclease, seminal, 2'-DEOXYCYTIDINE-2'-DEOXYADENOSINE-3',5'-MONOPHOSPHATE (3 entities in total)
• 機能のキーワード: ribonucleases, protein dynamics, protein structure-function, ligand binding, population shift, 3d domain swapping, hydrolase
• 由来する生物種: Bos taurus (cattle)
• 細胞内の位置: Secreted: P00669
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 28346.13

構造登録者

Merlino, A.,Vitagliano, L.,Sica, F.,Zagari, A.,Mazzarella, L. (登録日: 2003-10-10, 公開日: 2004-04-13, 最終更新日: 2024-10-30)

主引用文献

Merlino, A.,Vitagliano, L.,Sica, F.,Zagari, A.,Mazzarella, L.
Population shift vs induced fit: The case of bovine seminal ribonuclease swapping dimer
Biopolymers, 73:689-695, 2004

PubMed Abstract: Bovine seminal ribonuclease (BS-RNase) is a unique member of the pancreatic-like ribonuclease superfamily. This enzyme exists as two conformational isomers with distinctive biological properties. The structure of the major isomer is characterized by the swapping of the N-terminal segment (MxM BS-RNase). In this article, the crystal structures of the ligand-free MxM BS-RNase and its complex with 2'-deoxycitidylyl(3',5')-2'-deoxyadenosine derived from isomorphous crystals have been refined. Interestingly, the comparison between this novel ligand-free form and the previously published sulfate-bound structure reveals significant differences. In particular, the ligand-free MxM BS-RNase is closer to the structure of MxM BS-RNase productive complexes than to the sulfate-bound form. These results reveal that MxM BS-RNase presents a remarkable flexibility, despite the structural constraints of the interchain disulfide bridges and the swapping of the N-terminal helices. These findings have important implications to the ligand binding mechanism of MxM BS-RNase. Indeed, a population shift rather than a substrate-induced conformational transition may occur in the MxM BS-RNase ligand binding process.

PubMed: 15048772
DOI: 10.1002/bip.20016

実験手法

X-RAY DIFFRACTION (2.1 Å)