PDBsum entry 6klc

Viral protein

PDB id: 6klc

Contents

Protein chain

1436 a.a.

Metals

_MN

PDB id:

6klc

Name:

Viral protein

Title:

Structure of apo lassa virus polymerase

Structure:

RNA-directed RNA polymerase l. Chain: a. Synonym: protein l,large structural protein,replicase,transcriptase. Engineered: yes

Source:

Lassa mammarenavirus. Organism_taxid: 11620. Expressed in: spodoptera aff. Frugiperda 1 bold-2017. Expression_system_taxid: 2449148. Expression_system_cell_line: hifive

Authors:

R.Peng,X.Xu,J.Jing,Q.Peng,G.F.Gao,Y.Shi

Key ref:

R.Peng et al. (2020). Structural insight into arenavirus replication machinery. Nature, 579, 615-619. PubMed id: 32214249 DOI: 10.1038/s41586-020-2114-2

Date:

30-Jul-19 Release date: 18-Mar-20

Protein chain

A0A097F4L1  (A0A097F4L1_LASV) -  RNA-directed RNA polymerase L from Mammarenavirus lassaense

Seq: 2218 a.a.

Struc: 1436 a.a.

Enzyme reactions

• Enzyme class 2: E.C.2.7.7.48 - RNA-directed Rna polymerase.
• Reaction: RNA(n) + a ribonucleoside 5'-triphosphate = RNA(n+1) + diphosphate
• Enzyme class 3: E.C.3.1.-.-

Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

Added reference

DOI no: 10.1038/s41586-020-2114-2

Nature 579:615-619 (2020)

PubMed id: 32214249

Structural insight into arenavirus replication machinery.

R.Peng, X.Xu, J.Jing, M.Wang, Q.Peng, S.Liu, Y.Wu, X.Bao, P.Wang, J.Qi, G.F.Gao, Y.Shi.

ABSTRACT

Arenaviruses can cause severe haemorrhagic fever and neurological diseases in humans and other animals, exemplified by Lassa mammarenavirus, Machupo mammarenavirus and lymphocytic choriomeningitis virus, posing great threats to public health^1-4. These viruses encode a large multi-domain RNA-dependent RNA polymerase for transcription and replication of the viral genome⁵. Viral polymerases are one of the leading antiviral therapeutic targets. However, the structure of arenavirus polymerase is not yet known. Here we report the near-atomic resolution structures of Lassa and Machupo virus polymerases in both apo and promoter-bound forms. These structures display a similar overall architecture to influenza virus and bunyavirus polymerases but possess unique local features, including an arenavirus-specific insertion domain that regulates the polymerase activity. Notably, the ordered active site of arenavirus polymerase is inherently switched on, without the requirement for allosteric activation by 5'-viral RNA, which is a necessity for both influenza virus and bunyavirus polymerases^6,7. Moreover, dimerization could facilitate the polymerase activity. These findings advance our understanding of the mechanism of arenavirus replication and provide an important basis for developing antiviral therapeutics.