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The Open Protein Structure Annotation Network
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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

    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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