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PDBsum entry 2r7t
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Transferase/RNA
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PDB id
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2r7t
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Contents |
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* Residue conservation analysis
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Enzyme class:
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E.C.2.7.7.48
- RNA-directed Rna polymerase.
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Reaction:
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RNA(n) + a ribonucleoside 5'-triphosphate = RNA(n+1) + diphosphate
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RNA(n)
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+
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ribonucleoside 5'-triphosphate
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=
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RNA(n+1)
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+
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diphosphate
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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Structure
16:1678-1688
(2008)
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PubMed id:
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Mechanism for coordinated RNA packaging and genome replication by rotavirus polymerase VP1.
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X.Lu,
S.M.McDonald,
M.A.Tortorici,
Y.J.Tao,
R.Vasquez-Del Carpio,
M.L.Nibert,
J.T.Patton,
S.C.Harrison.
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ABSTRACT
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Rotavirus RNA-dependent RNA polymerase VP1 catalyzes RNA synthesis within a
subviral particle. This activity depends on core shell protein VP2. A conserved
sequence at the 3' end of plus-strand RNA templates is important for polymerase
association and genome replication. We have determined the structure of VP1 at
2.9 A resolution, as apoenzyme and in complex with RNA. The cage-like enzyme is
similar to reovirus lambda3, with four tunnels leading to or from a central,
catalytic cavity. A distinguishing characteristic of VP1 is specific
recognition, by conserved features of the template-entry channel, of four bases,
UGUG, in the conserved 3' sequence. Well-defined interactions with these bases
position the RNA so that its 3' end overshoots the initiating register,
producing a stable but catalytically inactive complex. We propose that specific
3' end recognition selects rotavirus RNA for packaging and that VP2 activates
the autoinhibited VP1/RNA complex to coordinate packaging and genome replication.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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S.M.McDonald,
and
J.T.Patton
(2011).
Assortment and packaging of the segmented rotavirus genome.
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Trends Microbiol,
19,
136-144.
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B.McClain,
E.Settembre,
B.R.Temple,
A.R.Bellamy,
and
S.C.Harrison
(2010).
X-ray crystal structure of the rotavirus inner capsid particle at 3.8 A resolution.
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J Mol Biol,
397,
587-599.
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PDB code:
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S.L.Noton,
V.M.Cowton,
C.R.Zack,
D.R.McGivern,
and
R.Fearns
(2010).
Evidence that the polymerase of respiratory syncytial virus initiates RNA replication in a nontemplated fashion.
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Proc Natl Acad Sci U S A,
107,
10226-10231.
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W.Li,
E.Manktelow,
J.C.von Kirchbach,
J.R.Gog,
U.Desselberger,
and
A.M.Lever
(2010).
Genomic analysis of codon, sequence and structural conservation with selective biochemical-structure mapping reveals highly conserved and dynamic structures in rotavirus RNAs with potential cis-acting functions.
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Nucleic Acids Res,
38,
7718-7735.
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A.A.Demidenko,
and
M.L.Nibert
(2009).
Probing the transcription mechanisms of reovirus cores with molecules that alter RNA duplex stability.
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J Virol,
83,
5659-5670.
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S.M.McDonald,
D.Aguayo,
F.D.Gonzalez-Nilo,
and
J.T.Patton
(2009).
Shared and group-specific features of the rotavirus RNA polymerase reveal potential determinants of gene reassortment restriction.
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J Virol,
83,
6135-6148.
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A.Shatkin,
K.Das,
and
E.Arnold
(2008).
3D jigsaw puzzle in rotavirus assembly.
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Structure,
16,
1601-1602.
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
code is
shown on the right.
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