PDBsum entry 5a22

Transferase

PDB id: 5a22

Contents

Protein chain

2002 a.a.

Metals

_ZN ×2

PDB id:

5a22

Name:

Transferase

Title:

Structure of the l protein of vesicular stomatitis virus from electron cryomicroscopy

Structure:

Vesicular stomatitis virus l polymerase. Chain: a. Engineered: yes

Source:

Vesicular stomatitis virus. Organism_taxid: 11276. Strain: indiana. Variant: san juan isolate. Expressed in: spodoptera frugiperda. Expression_system_taxid: 7108. Expression_system_cell_line: sf21.

Authors:

B.Liang,Z.Li,S.Jenni,A.A.Rameh,B.M.Morin,T.Grant,N.Grigorieff, S.C.Harrison,S.P.J.Whelan

Key ref:

B.Liang et al. (2015). Structure of the L Protein of Vesicular Stomatitis Virus from Electron Cryomicroscopy. Cell, 162, 314-327. PubMed id: 26144317 DOI: 10.1016/j.cell.2015.06.018

Date:

06-May-15 Release date: 19-Aug-15

Protein chain

P03523  (L_VSIVA) -  RNA-directed RNA polymerase L from Vesicular stomatitis Indiana virus (strain San Juan)

Seq: 2109 a.a.

Struc: 2002 a.a.*

* PDB and UniProt seqs differ at 7 residue positions (black crosses)

Enzyme reactions

• Enzyme class 2: E.C.2.1.1.375 - Nns virus cap methyltransferase.
• Reaction: a 5'-end (5'-triphosphoguanosine)-adenylyl-adenylyl-cytidylyl-adenosine in mRNA + 2 S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-(2'-O-methyladenylyl)-adenylyl-cytidylyl- adenosine in mRNA + 2 S-adenosyl-L-homocysteine + H⁺
• Enzyme class 3: E.C.2.7.7.48 - RNA-directed Rna polymerase.
• Reaction: RNA(n) + a ribonucleoside 5'-triphosphate = RNA(n+1) + diphosphate
• Enzyme class 4: E.C.2.7.7.88 - Gdp polyribonucleotidyltransferase.
• Reaction: a 5'-end triphospho-adenylyl-adenylyl-cytidylyl-adenosine in mRNA + GDP + H⁺ = a 5'-end (5'-triphosphoguanosine)-adenylyl-adenylyl-cytidylyl- adenosine in mRNA + diphosphate
• Enzyme class 5: E.C.3.6.1.- - ?????

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

reference

DOI no: 10.1016/j.cell.2015.06.018

Cell 162:314-327 (2015)

PubMed id: 26144317

Structure of the L Protein of Vesicular Stomatitis Virus from Electron Cryomicroscopy.

B.Liang, Z.Li, S.Jenni, A.A.Rahmeh, B.M.Morin, T.Grant, N.Grigorieff, S.C.Harrison, S.P.Whelan.

ABSTRACT

The large (L) proteins of non-segmented, negative-strand RNA viruses, a group that includes Ebola and rabies viruses, catalyze RNA-dependent RNA polymerization with viral ribonucleoprotein as template, a non-canonical sequence of capping and methylation reactions, and polyadenylation of viral messages. We have determined by electron cryomicroscopy the structure of the vesicular stomatitis virus (VSV) L protein. The density map, at a resolution of 3.8 Å, has led to an atomic model for nearly all of the 2109-residue polypeptide chain, which comprises three enzymatic domains (RNA-dependent RNA polymerase [RdRp], polyribonucleotidyl transferase [PRNTase], and methyltransferase) and two structural domains. The RdRp resembles the corresponding enzymatic regions of dsRNA virus polymerases and influenza virus polymerase. A loop from the PRNTase (capping) domain projects into the catalytic site of the RdRp, where it appears to have the role of a priming loop and to couple product elongation to large-scale conformational changes in L.