2R7O

Crystal Structure of VP1 apoenzyme of Rotavirus SA11 (N-terminal hexahistidine-tagged)

Summary for 2R7O

• Entry DOI: 10.2210/pdb2r7o/pdb
• Related: 2R7Q 2R7R 2R7S 2R7T 2R7U 2R7V 2R7W 2R7X
• Descriptor: RNA-dependent RNA polymerase (1 entity in total)
• Functional Keywords: viral protein, rna-dependent rna polymerase, single subunit polymerase fold, fingers, palm, thumb, right hand configuration, rna-directed rna polymerase, transferase
• Biological source: Simian rotavirus
• Cellular location: Virion : O37061
• Total number of polymer chains: 1
• Total formula weight: 126324.48

Authors

Lu, X.,Harrison, S.C.,Tao, Y.J.,Patton, J.T.,Nibert, M.L. (deposition date: 2007-09-09, release date: 2008-07-29, Last modification date: 2024-02-21)

Primary citation

Lu, 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

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

Experimental method

X-RAY DIFFRACTION (3.35 Å)