Mechanism for coordinated RNA packaging and genome replication by rotavirus polymerase VP1.
Mechanism for coordinated RNA packaging and genome replication by rotavirus polymerase VP1.
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DOI：
10.1016/j.str.2008.09.006
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发表时间：
2008-11-12
期刊：
影响因子：
--
通讯作者：
Harrison SC
中科院分区：
文献类型：
--
作者：
Lu X;McDonald SM;Tortorici MA;Tao YJ;Vasquez-Del Carpio R;Nibert ML;Patton JT;Harrison SC
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 Å resolution, as apoenzyme and in complex with RNA. The cage-like enzyme is similar to reovirus λ3, 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 auto-inhibited VP1/RNA complex to coordinate packaging and genome replication.
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DOI：
10.1073/pnas.90.13.6320
发表时间：
1993-07-01
影响因子：
11.1
作者：
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通讯作者：
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DOI：
10.1107/s0907444998003254
发表时间：
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期刊：
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影响因子：
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作者：
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DOI：
10.1107/s0907444997011980
发表时间：
1998-07-01
影响因子：
2.2
作者：
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通讯作者：
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影响因子：
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作者：
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