4UD0

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

Summary for 4UD0

• Entry DOI: 10.2210/pdb4ud0/pdb
• Related: 4UCI 4UCJ 4UCK 4UCL 4UCY 4UCZ
• Descriptor: RNA-DIRECTED RNA POLYMERASE L, SULFATE ION, ZINC ION, ... (5 entities in total)
• Functional Keywords: transferase, capping, l protein, rossmann, triphosphatase
• Biological source: HUMAN METAPNEUMOVIRUS
• Total number of polymer chains: 1
• Total formula weight: 48174.97

Authors

Paesen, G.C.,Collet, A.,Sallamand, C.,Debart, F.,Vasseur, J.J.,Canard, B.,Decroly, E.,Grimes, J.M. (deposition date: 2014-12-05, release date: 2015-11-18, Last modification date: 2024-05-08)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (3.2 Å)