

@article {778,
	title = {Mechanism for coordinated {RNA} packaging and genome replication by rotavirus polymerase {VP1.}},
	journal = {Structure {(London,} England : 1993)},
	volume = {16},
	number = {11},
	year = {2008},
	pages = {1678-1688},
	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{\textquoteright} 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{\textquoteright} sequence. Well-defined interactions with these bases position the {RNA} so that its 3{\textquoteright} end overshoots the initiating register, producing a stable but catalytically inactive complex. We propose that specific 3{\textquoteright} end recognition selects rotavirus {RNA} for packaging and that {VP2} activates the autoinhibited {VP1/RNA} complex to coordinate packaging and genome replication.},
	doi = {10.1016/j.str.2008.09.006},
	url = {http://dx.doi.org/10.1016/j.str.2008.09.006},
	author = {Lu, Xiaohui and McDonald, Sarah M and Tortorici, MA and Tao, Yizhi J and Vasquez-Del Carpio, Rodrigo and Nibert, Max L and Patton, John T and Harrison, Stephen C}
}
