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The Open Protein Structure Annotation Network
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1rhx

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

    Title NMR structure of the conserved hypothetical protein TM0979 from Thermotoga maritima. Proteins 59 387-390 2005
    Site JCSG
    PDB Id 1rhx Target Id 282848
    Molecular Characteristics
    Source Thermotoga maritima msb8
    Alias Ids TPS1250,TM0979, 84737 Molecular Weight 9875.84 Da.
    Residues 87 Isoelectric Point 4.71
    Sequence malvlvkygtdhpveklkirsakaedkivliqngvfwaleeletpakvyaikddflargyseedskvpl itysefidllegeekfig
      BLAST   FFAS

    Structure Determination
    Method NMR Chains 1

    Ligand Information
    Ligands
    Metals

    Jmol

     
    Google Scholar output for 1rhx
    1. Biomolecular NMR using a microcoil NMR probe-new technique for the chemical shift assignment of aromatic side chains in proteins
    W Peti, J Norcross, G Eldridge - Journal of the American , 2004 - ACS Publications
     
    2. Domain definition and target classification for CASP6
    M Tress, CH Tai, G Wang, I Ezkurdia - PROTEINS: , 2005 - Wiley Online Library
     
    3. Fast and accurate algorithms for protein side-chain packing
    J Xu, B Berger - Journal of the ACM (JACM), 2006 - dl.acm.org
     
    4. Protein structure prediction: The next generation
    MC Prentiss, C Hardin, MP Eastwood - Journal of Chemical , 2006 - ACS Publications
     
    5. NMR structure of the conserved hypothetical protein TM0979 from Thermotoga maritima
    W Peti, T Herrmann, O Zagnitko - Proteins: Structure, , 2005 - Wiley Online Library
     
    6. Microcoil NMR spectroscopy: a novel tool for biological high throughput NMR spectroscopy
    RE Hopson, W Peti - METHODS IN MOLECULAR BIOLOGY-CLIFTON , 2008 - Springer
     
    7. Protein structure prediction based on the sliced lattice model
    CC Wang, CB Yang, HY Ann - 2008 Conference on , 2005 - etd.lib.nsysu.edu.tw
     
    8. A replica exchange monte carlo algorithm for the optimization of secondary structure packing in proteins
    L Kapsokalivas, K Steinhfel - , Machine Learning and Data Mining in , 2010 - Springer
     
    9. Prediction of Protein Backbone Based on the Sliced Lattice Model
    CC Wang, CB Yang, HY Ann, HY Chang - 2008 - csie.npu.edu.tw
     
    10. Soft energy function and generic evolutionary method for discriminating native from nonnative protein conformations
    Y Chiu, J Hwang, J Yang - Journal of computational chemistry, 2008 - Wiley Online Library
     
    11. Stochastic local search for the optimization of secondary structure packing in proteins
    L Kapsokalivas - Learning and Intelligent Optimization, 2010 - Springer
     
    12. Protein Structure Prediction Using a Profile-Profile Comparison Method: FORTE
    _____ - ____, 2006 - J-STAGE
     
    13. Experiment planning for protein structure elucidation and site-directed protein recombination
    X Ye - 2007 - cs.dartmouth.edu
     

    Protein Summary

    The TM0979 gene of Thermotoga maritima belongs to the DsrH family of conserved bacterial proteins (Pfam04077, COG2168), which are involved in oxidation of intracellular sulfur but have no defined molecular function. Protein encoded by TM0979 has two NMR structures: 1RHX (PubMed:15723348 and 1X9A (PubMed:15608123). In Thermotoga maritima genome, two other open reading frames adjucent to TM0970 encode almost identical proteins.

    Other proteins involved in sulfur metabolism with sequence similarity to TM0979 are found as a component of heterohexameric complexes, such as DsrH from DsrEFH complex (PubMed:15687204) and TusB (tRNA 2-thiouridine synthesizing protein B)TusBCD complex (PubMed:16472754; DALI Z-score=9.8, RMSD=1.9 for 77 amino acids between PDB structures 1X9A:A and 2D1P:F).

    The TM0979 structure contains in the sequence order ?-?-?-?-?-?-(310)-?, where three-stranded parallel ?-sheet, located in the center of the protein is surrounded by the five helices (PubMed:15608123).

    Structure of TM0979 from T. maritima can be expected to contribute towards establishing the actual function of the DsrH protein and other members of this family potentially involved in sulfur metabolism.

    Figure 1. (attached below) TM0979 dimer (PDB id 1X9A) with surface colored according to sequence conservation in homologous proteins (red = conserved). Many conserved residues are clustered close to one side of the dimer interface as shown on the right side (subfigure D).

     

    Sulfur transferase activity predicted for DsrEFG based on conservation of catalytic residues/comparison with TusBCD [Ref].

    Ligand Summary



    References

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