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The Open Protein Structure Annotation Network
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3fkq

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

    Title Structure of the pilus assembly protein TadZ from Eubacterium rectale: implications for polar localization. Mol.Microbiol. 83 712-727 2012
    Site JCSG
    PDB Id 3fkq Target Id 389300
    Molecular Characteristics
    Source Eubacterium rectale atcc 33656
    Alias Ids TPS7599,YP_002936997.1, 382572 Molecular Weight 39814.50 Da.
    Residues 354 Isoelectric Point 4.94
    Sequence mkikvalldkdkeyldrltgvfntkyadklevysftdeknaiesvkeyridvliaeedfnidksefkrn cglayftgtpgielikdeiaickyqrvdvifkqilgvysdmaanvatisgendkssvviftspcggvgt stvaaacaiahanmgkkvfylnieqcgttdvffqaegnatmsdviyslksrkanlllklescikqsqeg vsyfsstkvaldileisyadidtligniqgmdnydeiivdlpfsleieklkllskawriivvndgsqls nykfmrayesvvlleqnddiniirnmnmiynkfsnknsemlsnisiktiggapryehatvrqiiealtk meffeeilq
      BLAST   FFAS

    Structure Determination
    Method XRAY Chains 1
    Resolution (Å) 2.10 Rfree 0.218
    Matthews' coefficent 3.09 Rfactor 0.190
    Waters 140 Solvent Content 60.25

    Ligand Information
    Ligands
    Metals

    Jmol

     
    Google Scholar output for 3fkq
    1. Mechanistic characterization of GS-9190 (Tegobuvir), a novel nonnucleoside inhibitor of hepatitis C virus NS5B polymerase
    I Shih, I Vliegen, B Peng, H Yang - Antimicrobial agents , 2011 - Am Soc Microbiol
     
    2. Structure of the pilus assembly protein TadZ from Eubacterium rectale: implications for polar localization
    Q Xu, B Christen, HJ Chiu, L Jaroszewski - Molecular , 2012 - Wiley Online Library
     
    3. Surface_based protein binding pocket similarity
    R Spitzer, AE Cleves, AN Jain - Proteins: Structure, Function, , 2011 - Wiley Online Library
     

    Protein Summary

    389300 is a novel protein with two domains, domain N (residues 1-114) and domain C (115:354). The N-terminal domain is a pseudo receiver domain, resembling the receiver domain in two component signaling systems. However, the pseudo receiver domain cannot be phosphorylated due to D->E mutation (E56). The molecular role of these pseudo receiver domains are not well understood. They are known to involve in circadian rhythm in bacteria and highly plants. The C-terminal  domain is ParA/SOJ ATPase-like, however, the Walker A (P-loop) is corrupted (K is mutated to T at position 140). As expected, the ATP bound cannot undergo hydrolysis, so 389300 is not an ATPase, but a pseudo ATPase. Thus, this protein is very interesting in that it is a concatenation of two "pseudo" domains. The C-terminal domain is likely involved in the dimerization of this protein. There are only a few protein sequences with this kind of arrangement. Genomics neighbour analysis suggests this protein is probably related to pillus assembly.

     

    Fig 1. monomer of 389300, ATP and other solvents are shown in sticks

    pk14342a-monomer.png

     

    Fig 2. monomer of 389300, ATP shown as spheres

     

    pk14342a-dimer.png

     

     

    Ligand Summary

    ATP and Mg bound to a site where P-loop is corrupted.

    Reviews

    References

     

    No references found.

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    Files (2)

    FileSizeDateAttached by 
     pk14342a-dimer.png
    dimer of 389300
    86.1 kB23:15, 25 Nov 2008qxuActions
     pk14342a-monomer.png
    monomer of 389300
    71.88 kB23:15, 25 Nov 2008qxuActions
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