2CJQ

Bovine viral diarrhea virus CP7-R12 RNA-dependent RNA polymerase

2CJQ の概要

• エントリーDOI: 10.2210/pdb2cjq/pdb
• 関連するPDBエントリー: 2AJJ 2AJM 2AJN 2AJO
• 分子名称: RNA-DIRECTED RNA POLYMERASE (2 entities in total)
• 機能のキーワード: transferase, rna-dependent rna polymerase, nucleotidyltransferase, bovine viral diarrhea virus, bvdv, helicase, membrane, protease, hydrolase, rna-directed rna polymerase, viral polymerase, nucleotide-binding, transmembrane, thiol protease, serine protease, atp-binding, polyprotein, glycoprotein
• 由来する生物種: BOVINE VIRAL DIARRHEA VIRUS (BVDV)
• 細胞内の位置: E(rns) glycoprotein: Host membrane; Peripheral membrane protein. Envelope glycoprotein E2: Host cell surface (By similarity). Cysteine protease NS2: Host membrane; Multi- pass membrane protein (Potential): Q96662
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 82302.22

構造登録者

Choi, K.H.,Gallei, A.,Becher, P.,Rossmann, M.G. (登録日: 2006-04-05, 公開日: 2006-07-19, 最終更新日: 2023-12-13)

主引用文献

Choi, K.H.,Gallei, A.,Becher, P.,Rossmann, M.G.
The Structure of Bovine Viral Diarrhea Virus RNA-Dependent RNA Polymerase and its Amino-Terminal Domain.
Structure, 14:1107-, 2006

PubMed Abstract: Viral RNA-dependent RNA polymerases (RdRp) differ from DNA-dependent RNA polymerases, DNA-dependent DNA polymerases, and reverse transcriptases in that RdRps contain "fingertips" consisting of several polypeptide strands in the fingers domain interacting with the thumb domain. The crystal structure of bovine viral diarrhea virus (BVDV) RdRp containing an Asn438 duplication shows that the "N-terminal domain," which occurs only in pestiviruses such as BVDV, interacts with the polymerase component of the same polypeptide chain. This contrasts with the domain swapping observed in the previously determined structure of the BVDV NADL strain RdRp. By comparison with the NADL structure and through the use of biochemical data, it is possible that the N-terminal domain, in conjunction with the fingertips, is required to bind and assist the translocation of the RNA template. The partial disorder of the loop containing the additional Asn438 residue may explain the low replication rate of the recombinant compared with the wild-type virus.

PubMed: 16843892
DOI: 10.1016/J.STR.2006.05.020

実験手法

X-RAY DIFFRACTION (2.6 Å)