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2p5z

    Table of contents
    1. 1. Protein Summary
    2. 2. Ligand Summary

    Title Type VI secretion apparatus and phage tail-associated protein complexes share a common evolutionary origin. Proc.Natl.Acad.Sci.Usa 106 4154-4159 2009
    Site NYSGXRC
    PDB Id 2p5z Target Id
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    Molecular Characteristics
    Source
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    Alias Ids
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    TPS7964,Q8FED2, PF04524
    Molecular Weight
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    Da.
    Residues
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    Isoelectric Point
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    Sequence
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      BLAST   FFAS

    Structure Determination
    Method XRAY
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    Chains 1
    Resolution (Å)
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    Rfree
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    Matthews' coefficent 2.83 Rfactor 0.217
    Waters
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    Solvent Content 56.47

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    Ligand Information
    Ligands
    Metals

    Jmol

     
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    Google Scholar output for 2p5z
    1. Type VI secretion apparatus and phage tail-associated protein complexes share a common evolutionary origin
    PG Leiman, M Basler, UA Ramagopal - Proceedings of the , 2009 - National Acad Sciences
     
    2. A common evolutionary origin for tailed-bacteriophage functional modules and bacterial machineries
    D Veesler, C Cambillau - Microbiology and Molecular Biology , 2011 - Am Soc Microbiol
     
    3. Structural basis for the secretion of EvpC: a key type VI secretion system protein from Edwardsiella tarda
    C Jobichen, S Chakraborty, M Li, J Zheng, L Joseph - PloS one, 2010 - dx.plos.org
     
    4. Structural biology of type VI secretion systems
    E Cascales, C Cambillau - of the Royal , 2012 - rstb.royalsocietypublishing.org
     
    5. The opening of the SPP1 bacteriophage tail, a prevalent mechanism in Gram-positive-infecting siphophages
    A Goulet, J Lai-Kee-Him, D Veesler, I Auzat - Journal of Biological , 2011 - ASBMB
     
    6. Phage Pierces the Host Cell Membrane with the Iron-Loaded Spike
    C Browning, MM Shneider, VD Bowman, D Schwarzer - Structure, 2012 - Elsevier
     
    7. Contractile Tail Machines of Bacteriophages
    PG Leiman, MM Shneider - Viral Molecular Machines, 2012 - Springer
     
    8. Phytobacterial Type VI secretion system-gene distribution, phylogeny, structure and biological functions
    PF Sarris, EA Trantas, N Skandalis - , Cumagun, CJ (Ed.), , 2012 - cdn.intechopen.com
     

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    Protein Summary

    The structure of the N-terminus of E. coli c3393 (VgrG) comprises 3 components of a type VI secretion system (T6SS) used by gram negative bacteria, which share structural similarity to bacteriophage gp27 tail proteins. The structure is published in PNAS (2009) by Leiman et al (Pubmed 19251641), and the authors propose that "T6SS is a multicomponent structure whose extracellular part resembles both structurally and functionally a bacteriophage tail, an efficient machine that translocates proteins and DNA across lipid membranes into cells."
     

     The 56 kDa protein that crystallized corresponds to residues 2-481 with a non-cleavable C-terminal His tag. The C-terminal half of the protein, starting around residue 490, is predicted to be a trimeric beta-helix, similar to the gp5 protein from the bacteriophage T4 cell-puncturing device published by Rossmann and coworkers (PDB:1k28, Pubmed: 11823865). Purification of full length VgrG has been unsuccessful (as of March 2009). 

    Ligand Summary

    Reviews

    References

     

    No references found.

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