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2R7T

Crystal Structure of Rotavirus SA11 VP1/RNA (UGUGAACC) Complex

Summary for 2R7T
Entry DOI10.2210/pdb2r7t/pdb
Related2R7O 2R7Q 2R7R 2R7S 2R7U 2R7V 2R7W 2R7X
DescriptorRNA (5'-R(*UP*GP*UP*GP*AP*AP*CP*C)-3'), RNA-dependent RNA polymerase (2 entities in total)
Functional Keywordsviral protein, rna-dependent rna polymerase, single subunit polymerase fold, fingers, palm, thumb, right hand configuration, rna-directed rna polymerase, transferase-rna complex, transferase/rna
Biological sourceSimian rotavirus
Cellular locationVirion : O37061
Total number of polymer chains2
Total formula weight128851.01
Authors
Lu, X.,Harrison, S.C.,Tao, Y.J.,Patton, J.T.,Nibert, M.L. (deposition date: 2007-09-10, release date: 2008-07-29, Last modification date: 2024-02-21)
Primary citationLu, X.,McDonald, S.M.,Tortorici, M.A.,Tao, Y.J.,Vasquez-Del Carpio, R.,Nibert, M.L.,Patton, J.T.,Harrison, S.C.
Mechanism for coordinated RNA packaging and genome replication by rotavirus polymerase VP1.
Structure, 16:1678-1688, 2008
Cited by
PubMed Abstract: 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.
PubMed: 19000820
DOI: 10.1016/j.str.2008.09.006
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3 Å)
Structure validation

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