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The Open Protein Structure Annotation Network
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1j5p

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

    Title Crystal structure of aspartate dehydrogenase (TM1643) from Thermotoga maritima at 1.9 A resolution. To be published
    Site JCSG
    PDB Id 1j5p Target Id 283500
    Molecular Characteristics
    Source Thermotoga maritima msb8
    Alias Ids TPS1307,TM1643, 85086 Molecular Weight 26638.52 Da.
    Residues 241 Isoelectric Point 7.75
    Sequence mtvliigmgnigkklvelgnfekiyaydriskdipgvvrldefqvpsdvstvvecaspeavkeyslqil knpvnyiiistsafadevfrerffselknsparvffpsgaiggldvlssikdfvknvrietikppkslg ldlkgktvvfegsveeasklfprninvastiglivgfekvkvtivadpamdhnihivrissaignyefk ienipspenpktsmltvysilrtlrnleskiifg
      BLAST   FFAS

    Structure Determination
    Method XRAY Chains 1
    Resolution (Å) 1.90 Rfree 0.26
    Matthews' coefficent 2.29 Rfactor 0.224
    Waters 82 Solvent Content 45.90

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    Ligand Information
    Ligands
    Metals

    Jmol

     
    Google Scholar output for 1j5p
    1. Progress of structural genomics initiatives: an analysis of solved target structures
    AE Todd, RL Marsden, JM Thornton - Journal of molecular , 2005 - Elsevier
     
    2. Statistical analysis and prediction of proteinprotein interfaces
    AJ Bordner, R Abagyan - Proteins: Structure, Function, and , 2005 - Wiley Online Library
     
    3. Microbial biochemistry, physiology, and biotechnology of hyperthermophilic Thermotoga species
    SB Conners, EF Mongodin, MR Johnson - FEMS microbiology , 2006 - Wiley Online Library
     
    4. Finding functional sites in structural genomics proteins
    A Stark, A Shkumatov, RB Russell - Structure, 2004 - Elsevier
     
    5. Aspartate dehydrogenase, a novel enzyme identified from structural and functional studies of TM1643
    Z Yang, A Savchenko, A Yakunin, R Zhang - Journal of Biological , 2003 - ASBMB
     
    6. Exploring structurally conserved solvent sites in protein families
    CA Bottoms, TA White, JJ Tanner - : Structure, Function, and , 2006 - Wiley Online Library
     
    7. Active site identification through geometry-based and sequence profile-based calculations: burial of catalytic clefts
    R Greaves, J Warwicker - Journal of molecular biology, 2005 - Elsevier
     
    8. Efficient recognition of protein fold at low sequence identity by conservative application of Psi_BLAST: validation
    FJ Stevens - Journal of Molecular Recognition, 2005 - Wiley Online Library
     
    9. Crystal structure of archaeal highly thermostable L_aspartate dehydrogenase/NAD/citrate ternary complex
    K Yoneda, H Sakuraba, H Tsuge, N Katunuma - FEBS , 2007 - Wiley Online Library
     
    10. Bioinformatics of protein bound water
    CA Bottoms - 2005 - mospace.umsystem.edu
     
    11. Carbohydrate utilization pathway analysis in the hyperthermophile Thermotoga maritima
    SB Conners - 2006 - repository.lib.ncsu.edu
     

    Protein Summary

     The gene TM1643 from Thermotoga maritima encodes an enzyme aspartate dehydrogenase EC:1.4.1.21 COG:COG0136.  The structure of this enzyme has been previously solved PDB:1H2H [Ref].  TM1643 is found in an operon with two other genes that encode enzymes involved in the biosynthesis of NAD.  The structure, 1j5p, contains a N-terminal Rossmann fold domain with a bound NAD(+) cofactor and a C-terminal alpha+beta DUF108 (SCOP). The active site of the enzyme is located at the interface between the two domains.  The enzyme is highly specific for aspartate and does not oxidize the similar amino acids glutamate and asparagine.  Other bacteria use oxidation of glutamate and asparagine as the first steps of de novo NAD biosynthesis.  In contrast, Thermotoga maritima uses NAD as a cofactor in the first step towards the synthesis of NAD ( PSI-SGKB).

    Ligand Summary



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