3EZK

Bacteriophage T4 gp17 motor assembly based on crystal structures and cryo-EM reconstructions


Experimental Data Snapshot

  • Method: ELECTRON MICROSCOPY
  • Resolution: 34.0 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

The structure of the phage T4 DNA packaging motor suggests a mechanism dependent on electrostatic forces.

Sun, S.Kondabagil, K.Draper, B.Alam, T.I.Bowman, V.D.Zhang, Z.Hegde, S.Fokine, A.Rossmann, M.G.Rao, V.B.

(2008) Cell 135: 1251-1262

  • DOI: https://doi.org/10.1016/j.cell.2008.11.015
  • Primary Citation of Related Structures:  
    3C6A, 3C6H, 3CPE, 3EZK

  • PubMed Abstract: 

    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.


  • Organizational Affiliation

    Department of Biological Sciences, Purdue University, 915 W. State Street, West Lafayette, IN 47907-2054, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
DNA packaging protein Gp17
A, B, C, D, E
577Tequatrovirus T4Mutation(s): 0 
Gene Names: 17
UniProt
Find proteins for P17312 (Enterobacteria phage T4)
Explore P17312 
Go to UniProtKB:  P17312
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP17312
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: ELECTRON MICROSCOPY
  • Resolution: 34.0 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 
EM Software:
TaskSoftware PackageVersion
RECONSTRUCTIONSPIDER

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2009-01-13
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Version format compliance
  • Version 1.2: 2018-07-18
    Changes: Data collection
  • Version 1.3: 2023-12-27
    Changes: Data collection, Database references, Refinement description