2R7W: Crystal Structure Of Rotavirus Sa11 Vp1/rna (ugugacc)/mrna 5'-cap (m7gpppg) Complex

Citation:
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.
PDB ID: 2R7WDownload
MMDB ID: 65687
PDB Deposition Date: 2007/9/10
Updated in MMDB: 2017/11
Experimental Method:
x-ray diffraction
Resolution: 2.6  Å
Source Organism:
Simian rotavirus
Similar Structures:
Biological Unit for 2R7W: dimeric; determined by author and by software (PISA)
Molecular Components in 2R7W
Label Count Molecule
Protein (1 molecule)
1
RNA-dependent RNA Polymerase
Molecule annotation
Nucleotide(1 molecule)
1
RNA (5'-r(*up*gp*up*gp*ap*cp*c)-3')
Molecule annotation
Chemical (1 molecule)
1
1
* Click molecule labels to explore molecular sequence information.

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