Unknown

Dataset Information

0

Structure of the bacteriophage phi29 DNA packaging motor.


ABSTRACT: Motors generating mechanical force, powered by the hydrolysis of ATP, translocate double-stranded DNA into preformed capsids (proheads) of bacterial viruses and certain animal viruses. Here we describe the motor that packages the double-stranded DNA of the Bacillus subtilis bacteriophage phi29 into a precursor capsid. We determined the structure of the head-tail connector--the central component of the phi29 DNA packaging motor--to 3.2 A resolution by means of X-ray crystallography. We then fitted the connector into the electron densities of the prohead and of the partially packaged prohead as determined using cryo-electron microscopy and image reconstruction analysis. Our results suggest that the prohead plus dodecameric connector, prohead RNA, viral ATPase and DNA comprise a rotary motor with the head-prohead RNA-ATPase complex acting as a stator, the DNA acting as a spindle, and the connector as a ball-race. The helical nature of the DNA converts the rotary action of the connector into translation of the DNA.

SUBMITTER: Simpson AA 

PROVIDER: S-EPMC4151180 | BioStudies | 2000-01-01

REPOSITORIES: biostudies

Similar Datasets

2008-01-01 | S-EPMC2615250 | BioStudies
| S-EPMC2777743 | BioStudies
2019-01-01 | S-EPMC6765105 | BioStudies
2007-01-01 | S-EPMC1800307 | BioStudies
2017-01-01 | S-EPMC5522947 | BioStudies
2013-01-01 | S-EPMC3850062 | BioStudies
2006-01-01 | S-EPMC1630414 | BioStudies
2013-01-01 | S-EPMC3753930 | BioStudies
2011-01-01 | S-EPMC3140409 | BioStudies
2007-01-01 | S-EPMC1976407 | BioStudies