A Charged Performance by gp17 in Viral Packaging | Zendy

R. Scott Williams | Zendy; Gareth J. Williams | Zendy; John A. Tainer | Zendy

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A Charged Performance by gp17 in Viral Packaging

Author(s) -

R. Scott Williams,

Gareth J. Williams,

John A. Tainer

Publication year - 2008

Publication title -

cell

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 26.304

H-Index - 776

eISSN - 1097-4172

pISSN - 0092-8674

DOI - 10.1016/j.cell.2008.12.011

Subject(s) - capsid , biology , molecular motor , nucleic acid , atp hydrolysis , energy metabolism , bacteriophage , biophysics , physics , atpase , biochemistry , genetics , enzyme , virus , gene , escherichia coli , endocrinology

Packaging of viral genomes into virus capsids requires powerful motors to overcome the repulsive force that builds as the nucleic acids are compressed. Through structural analyses of the T4 bacteriophage packaging motor gp17, Sun et al. (2008) now propose a packaging mechanism in which electrostatic forces cause the motor to alternate between tensed and relaxed conformational states.

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