2D7S

Foot and Mouth Disease Virus RNA-dependent RNA polymerase in complex with VPg protein

2D7S の概要

• エントリーDOI: 10.2210/pdb2d7s/pdb
• 関連するPDBエントリー: 1U09 1WNE
• 分子名称: RNA-dependent RNA polymerase, VPg1 protein (2 entities in total)
• 機能のキーワード: foot and mouth disease virus, rna-dependent rna polymerase, 3d polymerase, vpg, protein-primer, transferase
• 由来する生物種: Foot-and-mouth disease virus; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 55876.53

構造登録者

Ferrer-Orta, C.,Arias, A.,Perez-Luque, R.,Escarmis, C.,Domingo, E.,Verdaguer, N. (登録日: 2005-11-29, 公開日: 2006-03-28, 最終更新日: 2023-10-25)

主引用文献

Ferrer-Orta, C.,Arias, A.,Agudo, R.,Perez-Luque, R.,Escarmis, C.,Domingo, E.,Verdaguer, N.
The structure of a protein primer-polymerase complex in the initiation of genome replication
Embo J., 25:880-888, 2006

PubMed Abstract: Picornavirus RNA replication is initiated by the covalent attachment of a UMP molecule to the hydroxyl group of a tyrosine in the terminal protein VPg. This reaction is carried out by the viral RNA-dependent RNA polymerase (3D). Here, we report the X-ray structure of two complexes between foot-and-mouth disease virus 3D, VPg1, the substrate UTP and divalent cations, in the absence and in the presence of an oligoadenylate of 10 residues. In both complexes, VPg fits the RNA binding cleft of the polymerase and projects the key residue Tyr3 into the active site of 3D. This is achieved by multiple interactions with residues of motif F and helix alpha8 of the fingers domain and helix alpha13 of the thumb domain of the polymerase. The complex obtained in the presence of the oligoadenylate showed the product of the VPg uridylylation (VPg-UMP). Two metal ions and the catalytic aspartic acids of the polymerase active site, together with the basic residues of motif F, have been identified as participating in the priming reaction.

PubMed: 16456546
DOI: 10.1038/sj.emboj.7600971

実験手法

X-RAY DIFFRACTION (3 Å)