A critical coiled coil motif in the small terminase, gp16, from bacteriophage T4: insights into DNA packaging initiation and assembly of packaging motor.

doi:10.1016/j.jmb.2006.01.078

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Article

A critical coiled coil motif in the small terminase, gp16, from bacteriophage T4: insights into DNA packaging initiation and assembly of packaging motor.

Journal of molecular biology - 21 Apr 2006

Kondabagil Kiran R, Rao Venigalla B

Abstract excerpt

Double-stranded DNA packaging in bacteriophages is driven by one of the most powerful force-generating molecular motors reported to date. The phage T4 motor is composed of the small terminase protein, gpl6 (18kDa), the large terminase protein, gp17 (70kDa), and the dodecameric portal protein gp20 (61kDa). gp16, which exists as an oligomer in solution, is involved in the recognition of the viral DNA substrate, the...

Topics

Adenosine Triphosphatases
Amino Acid Motifs
Amino Acid Sequence
Bacteriophage T4
DNA Packaging
DNA-Binding Proteins
Endodeoxyribonucleases
Gene Expression
Hydrogen-Ion Concentration
Models, Molecular

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Molecular Motor Proteins

Molecular Sequence Data

Mutation

Protein Structure, Secondary

Sequence Alignment

Viral Proteins

Virus Assembly

Source

Open in PubMed

Identifiers

PMID: 16513134
DOI: 10.1016/j.jmb.2006.01.078

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