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The Open Protein Structure Annotation Network
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1vp2

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

    Title Crystal structure of Putative Xanthosine triphosphate pyrophosphatase1/HAM1 protein homolog (TM0159) from Thermotoga maritima at 1.78 A resolution. To be published
    Site JCSG
    PDB Id 1vp2 Target Id 282039
    Molecular Characteristics
    Source Thermotoga maritima msb8
    Alias Ids TPS1185,TM0159, 282361 Molecular Weight 22336.72 Da.
    Residues 196 Isoelectric Point 6.55
    Sequence mkkltvylattnphkveeikmiapewmeilpspekievvedgetflensvkkavvygkklkhpvmadds glviyslggfpgvmsarfmeehsykekmrtilkmlegkdrraafvcsatffdpventlisvedrvegri aneirgtggfgydpffipdgydktfgeiphlkekishrskafrklfsvlekilesenr
      BLAST   FFAS

    Structure Determination
    Method XRAY Chains 2
    Resolution (Å) 1.78 Rfree 0.20473
    Matthews' coefficent 2.53 Rfactor 0.16579
    Waters 256 Solvent Content 51.00

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    Ligand Information
    Ligands
    Metals

    Jmol

     
    Google Scholar output for 1vp2
    1. House cleaning, a part of good housekeeping
    MY Galperin, OV Moroz, KS Wilson - Molecular , 2006 - Wiley Online Library
     
    2. 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
     
    3. Crystal Structure of Human Inosine Triphosphatase
    P Stenmark, P Kursula, S Flodin, S Grslund - Journal of Biological , 2007 - ASBMB
     

    Protein Summary

    The TM0159 gene of Thermotoga maritima encodes the NP_227974 protein, a putative nonstandard nucleoside triphosphate pyrohydrolase (NTPase) (EC:3.6.1.23, PFAM:PF01725, COG:COG0127). It shows a possible functional linkage (score 0.8) with its genomic neighbor TM0161, a geranyltranstransferase.

    The structure of TM0159 monomer, 1vp2, adopts an anticodon-binding domain-like fold, inside the ITPase-like superfamily, ITPase/Ham1 family. According to DALI, 1vp2 shows strong similarity (main-chain rmsd 1.7 Å over 181 residues with 37% sequence identity, Dali Zscr=25) to the NTPase of another hyperthermophile, Pyrococcus horikoshii (PDB:2dvo ; and PDB:2dvp).The active site residues, as determined for the Pyrococcus ortholog (Lokanath 2008), are conserved in TM0159 (Fig. 1).

     

     1vp2_2dvo (1).png

     

     

    Figure 1. The active site of nonstandard NTPase. Stereo-ribbon view showing the structural superposition of the orthologs from T. maritima (PDB id: 1vp2, in magenta) and P. horikoshii (PDB id: 2dvo, in cyan). Residues within hydrogen-bonding distance of the ligand (inosine-5-triphosphate, in yellow) are indicated in ball-and-stick and labeled for 1vp2.

     

    Like in the Pyrococcus structure, the quaternary structure of 1vp2 forms a horseshoe-like homodimer. Dimerization has been suggested to play a role in regulating catalysis by affecting the active site conformation (Lokanath 2008).

    Ligand Summary



    References

    Reviews

    References

     

    No references found.

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