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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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References listed in PDB file
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Key reference
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Title
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Mechanism for coordinated RNA packaging and genome replication by rotavirus polymerase vp1.
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Authors
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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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Ref.
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Structure, 2008,
16,
1678-1688.
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PubMed id
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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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