1HHS

RNA dependent RNA polymerase from dsRNA bacteriophage phi6

1HHS の概要

• エントリーDOI: 10.2210/pdb1hhs/pdb
• 関連するPDBエントリー: 1HHT 1HI0 1HI1 1HI8
• 分子名称: RNA-DIRECTED RNA POLYMERASE, MANGANESE (II) ION (3 entities in total)
• 機能のキーワード: rna polymerase, viral polymerase, transferase
• 由来する生物種: BACTERIOPHAGE PHI-6 (PHAGE PHI 6)
• 細胞内の位置: Virion: P11124
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 224874.42

構造登録者

Grimes, J.M.,Butcher, S.J.,Makeyev, E.V.,Bamford, D.H.,Stuart, D.I. (登録日: 2000-12-28, 公開日: 2001-03-27, 最終更新日: 2024-05-08)

主引用文献

Butcher, S.J.,Grimes, J.M.,Makeyev, E.V.,Bamford, D.H.,Stuart, D.I.
A Mechanism for Initiating RNA-Dependent RNA Polymerization
Nature, 410:235-, 2001

PubMed Abstract: In most RNA viruses, genome replication and transcription are catalysed by a viral RNA-dependent RNA polymerase. Double-stranded RNA viruses perform these operations in a capsid (the polymerase complex), using an enzyme that can read both single- and double-stranded RNA. Structures have been solved for such viral capsids, but they do not resolve the polymerase subunits in any detail. Here we show that the 2 A resolution X-ray structure of the active polymerase subunit from the double-stranded RNA bacteriophage straight phi6 is highly similar to that of the polymerase of hepatitis C virus, providing an evolutionary link between double-stranded RNA viruses and flaviviruses. By crystal soaking and co-crystallization, we determined a number of other structures, including complexes with oligonucleotide and/or nucleoside triphosphates (NTPs), that suggest a mechanism by which the incoming double-stranded RNA is opened up to feed the template through to the active site, while the substrates enter by another route. The template strand initially overshoots, locking into a specificity pocket, and then, in the presence of cognate NTPs, reverses to form the initiation complex; this process engages two NTPs, one of which acts with the carboxy-terminal domain of the protein to prime the reaction. Our results provide a working model for the initiation of replication and transcription.

PubMed: 11242087
DOI: 10.1038/35065653

実験手法

X-RAY DIFFRACTION (2 Å)