Loading
PDBj
メニューPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

2PUS

Unprecedented activation mechanism of a non-canonical RNA-dependent RNA polymerase

2PUS の概要
エントリーDOI10.2210/pdb2pus/pdb
分子名称IBDV VP1 RNA-dependant RNA polymerase (2 entities in total)
機能のキーワードrna polymerase motifs, transferase
由来する生物種Infectious bursal disease virus (Gumboro virus)
細胞内の位置Virion (By similarity): Q9Q6Q5
タンパク質・核酸の鎖数1
化学式量合計94651.88
構造登録者
Garriga, D.,Navarro, A.,Querol-Audi, J.,Abaitua, F.,Rodriguez, J.F.,Verdaguer, N. (登録日: 2007-05-09, 公開日: 2007-11-27, 最終更新日: 2024-02-21)
主引用文献Garriga, D.,Navarro, A.,Querol-Audi, J.,Abaitua, F.,Rodriguez, J.F.,Verdaguer, N.
Activation mechanism of a noncanonical RNA-dependent RNA polymerase.
Proc.Natl.Acad.Sci.Usa, 104:20540-20545, 2007
Cited by
PubMed Abstract: Two lineages of viral RNA-dependent RNA polymerases (RDRPs) differing in the organization (canonical vs. noncanonical) of the palm subdomain have been identified. Phylogenetic analyses indicate that both lineages diverged at a very early stage of the evolution of the enzyme [Gorbalenya AE, Pringle FM, Zeddam JL, Luke BT, Cameron CE, Kalmakoff J, Hanzlik TN, Gordon KH, Ward VK (2002) J Mol Biol 324:47-62]. Here, we report the x-ray structure of a noncanonical birnaviral RDRP, named VP1, in its free form, bound to Mg(2+) ions, and bound to a peptide representing the polymerase-binding motif of the regulatory viral protein VP3. The structure of VP1 reveals that the noncanonical connectivity of the palm subdomain maintains the geometry of the catalytic residues found in canonical polymerases but results in a partial blocking of the active site cavity. The VP1-VP3 peptide complex shows a mode of polymerase activation in which VP3 binding promotes a conformational change that removes the steric blockade of the VP1 active site, facilitating the accommodation of the template and incoming nucleotides for catalysis. The striking structural similarities between birnavirus (dsRNA) and the positive-stranded RNA picornavirus and calicivirus RDRPs provide evidence supporting the existence of functional and evolutionary relationships between these two virus groups.
PubMed: 18077388
DOI: 10.1073/pnas.0704447104
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.4 Å)
構造検証レポート
Validation report summary of 2pus
検証レポート(詳細版)ダウンロードをダウンロード

250059

件を2026-03-04に公開中

PDB statisticsPDBj update infoContact PDBjnumon