2WNM

Solution structure of Gp2


Experimental Data Snapshot

  • Method: SOLUTION NMR
  • Conformers Calculated: 20 
  • Conformers Submitted: 
  • Selection Criteria: REPRESENTATIVE STRUCTURE 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

T7 Phage Protein Gp2 Inhibits the Escherichia Coli RNA Polymerase by Antagonizing Stable DNA Strand Separation Near the Transcription Start Site.

Camara, B.Liu, M.Reynolds, J.Shadrin, A.Liu, B.Kwok, K.Simpson, P.Weinzierl, R.Severinov, K.Cota, E.Matthews, S.Wigneshweraraj, S.R.

(2010) Proc Natl Acad Sci U S A 107: 2247

  • DOI: https://doi.org/10.1073/pnas.0907908107
  • Primary Citation of Related Structures:  
    2WNM

  • PubMed Abstract: 

    Infection of Escherichia coli by the T7 phage leads to rapid and selective inhibition of the host RNA polymerase (RNAP)--a multi-subunit enzyme responsible for gene transcription--by a small ( approximately 7 kDa) phage-encoded protein called Gp2. Gp2 is also a potent inhibitor of E. coli RNAP in vitro. Here we describe the first atomic resolution structure of Gp2, which reveals a distinct run of surface-exposed negatively charged amino acid residues on one side of the molecule. Our comprehensive mutagenesis data reveal that two conserved arginine residues located on the opposite side of Gp2 are important for binding to and inhibition of RNAP. Based on a structural model of the Gp2-RNAP complex, we propose that inhibition of transcription by Gp2 involves prevention of RNAP-promoter DNA interactions required for stable DNA strand separation and maintenance of the "transcription bubble" near the transcription start site, an obligatory step in the formation of a transcriptionally competent promoter complex.


  • Organizational Affiliation

    Department of Microbiology and Centre for Molecular Microbiology and Infection, Imperial College London, London SW7 2AZ, United Kingdom.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
GENE 264Escherichia phage T7Mutation(s): 0 
UniProt
Find proteins for P03704 (Escherichia phage T7)
Explore P03704 
Go to UniProtKB:  P03704
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP03704
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: SOLUTION NMR
  • Conformers Calculated: 20 
  • Conformers Submitted: 
  • Selection Criteria: REPRESENTATIVE STRUCTURE 

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2010-02-16
    Type: Initial release
  • Version 1.1: 2011-05-08
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2024-05-15
    Changes: Data collection, Database references, Other