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1vma

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

    Title Crystal structure of Cell division protein ftsY (TM0570) from Thermotoga maritima at 1.60 A resolution. To be published
    Site JCSG
    PDB Id 1vma Target Id 282443
    Molecular Characteristics
    Source Thermotoga maritima msb8
    Alias Ids TPS1216,TM0570, BIG_343, BIG_267, 89981 Molecular Weight 32044.51 Da.
    Residues 294 Isoelectric Point 5.48
    Sequence mglfdflkkglqktketffgrvvkllkgkklddetreeleelliqadvgvetteyilerleekdgdale slkeiileilnfdtklnvppeppfvimvvgvngtgkttscgklakmfvdegksvvlaaadtfraaaieq lkiwgervgatvishsegadpaavafdavahalarnkdvviidtagrlhtkknlmeelrkvhrvvkkki pdaphetllvidattgqnglvqakifkeavnvtgiiltkldgtakggitlaiarelgipikfigvgeka edlrpfdpeafvevllse
      BLAST   FFAS

    Structure Determination
    Method XRAY Chains 2
    Resolution (Å) 1.60 Rfree 0.2534
    Matthews' coefficent 2.39 Rfactor 0.20674
    Waters 394 Solvent Content 48.17

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    Ligand Information
    Ligands
    Metals

    Jmol

     
    Google Scholar output for 1vma
    1. Contribution of Electrostatic Interactions, Compactness and Quaternary Structure to Protein Thermostability: Lessons from Structural Genomics of Thermotoga
    M Robinson-Rechavi, A Alibs, A Godzik - Journal of molecular biology, 2006 - Elsevier
     
    2. Escherichia coli signal recognition particle receptor FtsY contains an essential and autonomous membrane-binding amphipathic helix
    R Parlitz, A Eitan, G Stjepanovic, L Bahari - Journal of Biological , 2007 - ASBMB
     
    3. X_ray structure of the T. Aquaticus Ftsy: GDP complex suggests functional roles for the C_terminal helix of the SRP GTPases
    J Gawronski_Salerno, JS Coon V - Proteins: Structure, , 2007 - Wiley Online Library
     
    4. The crystal structure of the third signal-recognition particle GTPase FlhF reveals a homodimer with bound GTP
    G Bange, G Petzold, K Wild - Proceedings of the , 2007 - National Acad Sciences
     
    5. Structure of the chloroplast signal recognition particle (SRP) receptor: domain arrangement modulates SRP-receptor interaction
    S Chandrasekar, J Chartron, P Jaru-Ampornpan - Journal of molecular , 2008 - Elsevier
     
    6. The structure of the chloroplast signal recognition particle (SRP) receptor reveals mechanistic details of SRP GTPase activation and a conserved membrane targeting
    KF Stengel, I Holdermann, K Wild, I Sinning - FEBS letters, 2007 - Elsevier
     
    7. Structures of the signal recognition particle receptor from the archaeon Pyrococcus furiosus: implications for the targeting step at the membrane
    PF Egea, H Tsuruta, GP De Leon, J Napetschnig - PLoS one, 2008 - dx.plos.org
     
    8. Conformational variability of the GTPase domain of the signal recognition particle receptor FtsY
    T Gariani, T Samuelsson, AE Sauer-Eriksson - Journal of structural biology, 2006 - Elsevier
     

    Protein Summary


    The TM0570 gene from Thermotoga maritima encodes a SRP54-type protein PF02881 COG0552.  The structure represents the N-terminal helical bundle domain of the 54 kDa SRP54 component, a GTP-binding protein that interacts with the signal sequence when it emerges from the ribosome. SRP54 of the signal recognition particle has a three-domain structure: an N-terminal helical bundle domain (Ffh), a GTPase domain (FtsY), and the M-domain that binds the 7s RNA and also binds the signal sequence.  The related structure from Thermus aquaticus is 2CNW. The signal recognition particles Ffh and FtsY play a central role in co-translational targeting of proteins, assembling in a GTP-dependent manner to generate the SRP targeting complex at the membrane. A suite of residues in FtsY have been identified that are essential for the hydrolysis of GTP that accompanies disengagement.  A direct interaction with RNA plays a role in regulating the activity of the SRP targeting complex.

    Ligand Summary



    References

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