1QEX

BACTERIOPHAGE T4 GENE PRODUCT 9 (GP9), THE TRIGGER OF TAIL CONTRACTION AND THE LONG TAIL FIBERS CONNECTOR


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.30 Å
  • R-Value Free: 0.277 
  • R-Value Work: 0.239 

wwPDB Validation   3D Report Full Report


This is version 1.5 of the entry. See complete history


Literature

The structure of bacteriophage T4 gene product 9: the trigger for tail contraction.

Kostyuchenko, V.A.Navruzbekov, G.A.Kurochkina, L.P.Strelkov, S.V.Mesyanzhinov, V.V.Rossmann, M.G.

(1999) Structure 7: 1213-1222

  • DOI: https://doi.org/10.1016/s0969-2126(00)80055-6
  • Primary Citation of Related Structures:  
    1QEX, 1S2E

  • PubMed Abstract: 

    The T4 bacteriophage consists of a head, filled with double-stranded DNA, and a complex contractile tail required for the ejection of the viral genome into the Escherichia coli host. The tail has a baseplate to whïch are attached six long and six short tail fibers. These fibers are the sensing devices for recognizing the host. When activated by attachment to cell receptors, the fibers cause a conformational transition in the baseplate and subsequently in the tail sheath, which initiates DNA ejection. The baseplate is a multisubunit complex of proteins encoded by 15 genes. Gene product 9 (gp9) is the protein that connects the long tail fibers to the baseplate and triggers the tail contraction after virus attachment to a host cell.


  • Organizational Affiliation

    Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry, 16/10 Miklukho-Maklaya Street, Moscow, 117871, Russia.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
PROTEIN (BACTERIOPHAGE T4 GENE PRODUCT 9 (GP9))
A, B
288Tequatrovirus T4Mutation(s): 0 
Gene Names: 9
UniProt
Find proteins for P10927 (Enterobacteria phage T4)
Explore P10927 
Go to UniProtKB:  P10927
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP10927
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 1 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
EPE
Query on EPE

Download Ideal Coordinates CCD File 
C [auth A],
D [auth B]
4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID
C8 H18 N2 O4 S
JKMHFZQWWAIEOD-UHFFFAOYSA-N
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.30 Å
  • R-Value Free: 0.277 
  • R-Value Work: 0.239 
  • Space Group: H 3 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 94.33α = 90
b = 94.33β = 90
c = 440.94γ = 120
Software Package:
Software NamePurpose
CCP4model building
CNSrefinement
DENZOdata reduction
SnBphasing
CCP4phasing

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1999-10-05
    Type: Initial release
  • Version 1.1: 2008-04-26
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Derived calculations, Version format compliance
  • Version 1.3: 2017-10-04
    Changes: Refinement description
  • Version 1.4: 2019-11-20
    Changes: Database references
  • Version 1.5: 2023-12-27
    Changes: Data collection, Database references, Derived calculations