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Structure paper

TitleThe structure of the phage T4 DNA packaging motor suggests a mechanism dependent on electrostatic forces.
Journal, issue, pagesCell, Vol. 135, Issue 7, Page 1251-1262, Year 2008
Publish dateDec 26, 2008
AuthorsSiyang Sun / Kiran Kondabagil / Bonnie Draper / Tanfis I Alam / Valorie D Bowman / Zhihong Zhang / Shylaja Hegde / Andrei Fokine / Michael G Rossmann / Venigalla B Rao /
PubMed AbstractViral genomes are packaged into "procapsids" by powerful molecular motors. We report the crystal structure of the DNA packaging motor protein, gene product 17 (gp17), in bacteriophage T4. The ...Viral genomes are packaged into "procapsids" by powerful molecular motors. We report the crystal structure of the DNA packaging motor protein, gene product 17 (gp17), in bacteriophage T4. The structure consists of an N-terminal ATPase domain, which provides energy for compacting DNA, and a C-terminal nuclease domain, which terminates packaging. We show that another function of the C-terminal domain is to translocate the genome into the procapsid. The two domains are in close contact in the crystal structure, representing a "tensed state." A cryo-electron microscopy reconstruction of the T4 procapsid complexed with gp17 shows that the packaging motor is a pentamer and that the domains within each monomer are spatially separated, representing a "relaxed state." These structures suggest a mechanism, supported by mutational and other data, in which electrostatic forces drive the DNA packaging by alternating between tensed and relaxed states. Similar mechanisms may occur in other molecular motors.
External linksCell / PubMed:19109896
MethodsEM (single particle) / X-ray diffraction
Resolution1.16 - 34.0 Å
Structure data

1572

3ezk

EMDB-1572: The T4 packaging motor, T4 procapsid with large terminase gp17 bound
PDB-3ezk: Bacteriophage T4 gp17 motor assembly based on crystal structures and cryo-EM reconstructions
Method: EM (single particle) / Resolution: 34.0 Å

EMDB-1573:
The bacteriophage T4 procapsid in the process of DNA packaging
Method: EM (single particle) / Resolution: 32.0 Å

PDB-3c6a:
Crystal Structure of the RB49 gp17 nuclease domain
Method: X-RAY DIFFRACTION / Resolution: 1.16 Å

PDB-3c6h:
Crystal Structure of the RB49 gp17 nuclease domain
Method: X-RAY DIFFRACTION / Resolution: 2.8 Å

PDB-3cpe:
Crystal Structure of T4 gp17
Method: X-RAY DIFFRACTION / Resolution: 2.8 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-PO4:
PHOSPHATE ION

ChemComp-NA:
Unknown entry

Source
  • enterobacteria phage rb49 (virus)
  • bacteriophage t4 (virus)
KeywordsVIRAL PROTEIN / terminase nuclease / HYDROLASE / large terminase / Alternative initiation / ATP-binding / DNA-binding / Nuclease / Nucleotide-binding / pentameric motor / DNA packaging

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