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PDBsum entry 5a22
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References listed in PDB file
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Key reference
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Title
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Structure of the l protein of vesicular stomatitis virus from electron cryomicroscopy.
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Authors
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B.Liang,
Z.Li,
S.Jenni,
A.A.Rahmeh,
B.M.Morin,
T.Grant,
N.Grigorieff,
S.C.Harrison,
S.P.Whelan.
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Ref.
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Cell, 2015,
162,
314-327.
[DOI no: ]
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PubMed id
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Abstract
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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.
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