2OIH

Hepatitis Delta Virus gemonic ribozyme precursor with C75U mutation and bound to monovalent cation Tl+

2OIH の概要

• エントリーDOI: 10.2210/pdb2oih/pdb
• 分子名称: HDV ribozyme, U1 small nuclear ribonucleoprotein A, THALLIUM (I) ION, ... (4 entities in total)
• 機能のキーワード: tl+-bound, structural protein-rna complex, structural protein/rna
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Nucleus: P09012
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 38725.57

構造登録者

Ke, A.,Ding, F.,Batchelor, J.D.,Doudna, J.A. (登録日: 2007-01-11, 公開日: 2007-03-27, 最終更新日: 2023-12-27)

主引用文献

Ke, A.,Ding, F.,Batchelor, J.D.,Doudna, J.A.
Structural roles of monovalent cations in the HDV ribozyme.
Structure, 15:281-287, 2007

PubMed Abstract: The hepatitis delta virus (HDV) ribozyme catalyzes viral RNA self-cleavage through general acid-base chemistry in which an active-site cytidine and at least one metal ion are involved. Monovalent metal ions support slow catalysis and were proposed to substitute for structural, but not catalytic, divalent metal ions in the RNA. To investigate the role of monovalent cations in ribozyme structure and function, we determined the crystal structure of the precursor HDV ribozyme in the presence of thallium ions (Tl(+)). Two Tl(+) ions can occupy a previously observed divalent metal ion hexahydrate-binding site located near the scissile phosphate, but are easily competed away by cobalt hexammine, a magnesium hexahydrate mimic and potent reaction inhibitor. Intriguingly, a third Tl(+) ion forms direct inner-sphere contacts with the ribose 2'-OH nucleophile and the pro-S(p) scissile phosphate oxygen. We discuss possible structural and catalytic implications of monovalent cation binding for the HDV ribozyme mechanism.

PubMed: 17355864
DOI: 10.1016/j.str.2007.01.017

実験手法

X-RAY DIFFRACTION (2.4 Å)