1L9V

Non Structural protein encoded by gene segment 8 of rotavirus (NSP2), an NTPase, ssRNA binding and nucleic acid helix-destabilizing protein

1L9V の概要

• エントリーDOI: 10.2210/pdb1l9v/pdb
• 分子名称: Rotavirus-NSP2 (2 entities in total)
• 機能のキーワード: alpha/beta protein, hit-like fold, octamer, two domain protein, viral protein
• 由来する生物種: Simian 11 rotavirus (serotype 3 / strain SA11-Ramig)
• 細胞内の位置: Host cytoplasm (Potential): Q03243
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 36618.26

構造登録者

Jayaram, H.,Taraporewala, Z.,Patton, J.T.,Prasad, B.V. (登録日: 2002-03-26, 公開日: 2002-06-05, 最終更新日: 2024-02-14)

主引用文献

Jayaram, H.,Taraporewala, Z.,Patton, J.T.,Prasad, B.V.
Rotavirus protein involved in genome replication and packaging exhibits a HIT-like fold.
Nature, 417:311-315, 2002

PubMed Abstract: Rotavirus, the major cause of life-threatening infantile gastroenteritis, is a member of the Reoviridae. Although the structures of rotavirus and other members of the Reoviridae have been extensively studied, little is known about the structures of virus-encoded non-structural proteins that are essential for genome replication and packaging. The non-structural protein NSP2 of rotavirus, which exhibits nucleoside triphosphatase, single-stranded RNA binding, and nucleic-acid helix-destabilizing activities, is a major component of viral replicase complexes. We present here the X-ray structure of the functional octamer of NSP2 determined to a resolution of 2.6 A. The NSP2 monomer has two distinct domains. The amino-terminal domain has a new fold. The carboxy-terminal domain resembles the ubiquitous cellular histidine triad (HIT) group of nucleotidyl hydrolases. This structural similarity suggests that the nucleotide-binding site is located inside the cleft between the two domains. Prominent grooves that run diagonally across the doughnut-shaped octamer are probable locations for RNA binding. Several RNA binding sites, resulting from the quaternary organization of NSP2 monomers, may be required for the helix destabilizing activity of NSP2 and its function during genome replication and packaging.

PubMed: 12015608
DOI: 10.1038/417311a

実験手法

X-RAY DIFFRACTION (2.6 Å)