Defining molecular and domain boundaries in the bacteriophage phi29 DNA packaging motor.
Defining molecular and domain boundaries in the bacteriophage phi29 DNA packaging motor.
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DOI:
10.1016/j.str.2008.05.010
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发表时间:
2008-08-06
期刊:
影响因子:
5.7
通讯作者:
Rossmann, Michael G.
中科院分区:
文献类型:
--
作者:
Morais, Marc C.;Koti, Jaya S.;Bowman, Valorie D.;Reyes-Aldrete, Emilio;Anderson, Dwight L.;Rossmann, Michael G.
Cryo-electron microscopy (cryoEM) studies of the bacteriophage ϕ29 DNA packaging motor have delineated the relative positions and molecular boundaries of the 12-fold symmetric head-tail connector, the 5-fold symmetric prohead RNA (pRNA), the ATPase that provides the energy for packaging, and the procapsid. Reconstructions, assuming 5-fold symmetry, were determined for proheads with 174-base, 120-base, 71-base pRNA, proheads lacking pRNA; proheads with ATPase bound, and proheads in which the packaging motor was missing the connector. These structures are consistent with pRNA and ATPase forming a pentameric motor component around the unique vertex of proheads. They suggest an assembly pathway for the packaging motor, and a mechanism for DNA translocation into empty proheads.
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