4UCZ

X-ray structure and activities of an essential Mononegavirales L- protein domain

4UCZ の概要

• エントリーDOI: 10.2210/pdb4ucz/pdb
• 関連するPDBエントリー: 4UCI 4UCJ 4UCK 4UCL 4UCY 4UD0
• 分子名称: RNA-DIRECTED RNA POLYMERASE L, ZINC ION, GUANOSINE-5'-TRIPHOSPHATE, ... (5 entities in total)
• 機能のキーワード: transferase, capping, l protein, rossmann, triphosphatase
• 由来する生物種: HUMAN METAPNEUMOVIRUS
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 96259.54

構造登録者

Paesen, G.C.,Collet, A.,Sallamand, C.,Debart, F.,Vasseur, J.J.,Canard, B.,Decroly, E.,Grimes, J.M. (登録日: 2014-12-05, 公開日: 2015-11-18, 最終更新日: 2024-10-16)

主引用文献

Paesen, G.C.,Collet, A.,Sallamand, C.,Debart, F.,Vasseur, J.J.,Canard, B.,Decroly, E.,Grimes, J.M.
X-Ray Structure and Activities of an Essential Mononegavirales L-Protein Domain.
Nat.Commun., 6:8749-, 2015

PubMed Abstract: The L protein of mononegaviruses harbours all catalytic activities for genome replication and transcription. It contains six conserved domains (CR-I to -VI; Fig. 1a). CR-III has been linked to polymerase and polyadenylation activity, CR-V to mRNA capping and CR-VI to cap methylation. However, how these activities are choreographed is poorly understood. Here we present the 2.2-Å X-ray structure and activities of CR-VI+, a portion of human Metapneumovirus L consisting of CR-VI and the poorly conserved region at its C terminus, the +domain. The CR-VI domain has a methyltransferase fold, which besides the typical S-adenosylmethionine-binding site ((SAM)P) also contains a novel pocket ((NS)P) that can accommodate a nucleoside. CR-VI lacks an obvious cap-binding site, and the (SAM)P-adjoining site holding the nucleotides undergoing methylation ((SUB)P) is unusually narrow because of the overhanging +domain. CR-VI+ sequentially methylates caps at their 2'O and N7 positions, and also displays nucleotide triphosphatase activity.

PubMed: 26549102
DOI: 10.1038/NCOMMS9749

実験手法

X-RAY DIFFRACTION (2.99 Å)