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

    Title Crystal structure of Dihydrodipicolinate reductase (TM1520) from Thermotoga maritima at 2.27 A resolution. To be published
    Site JCSG
    PDB Id 1vm6 Target Id 283377
    Molecular Characteristics
    Source Thermotoga maritima msb8
    Alias Ids TPS1295,TM1520, 282606 Molecular Weight 23730.22 Da.
    Residues 216 Isoelectric Point 5.70
    Sequence mkygivgysgrmgqeiqkvfsekghelvlkvdvngveeldspdvvidfsspealpktvdlckkyraglv lgttalkeehlqmlrelskevpvvqaynfsiginvlkrflselvkvledwdveivethhrfkkdapsgt aillesalgksvpihslrvggvpgdhvvvfgnigetieikhraisrtvfaigalkaaeflvgkdpgmys feevifgge
      BLAST   FFAS

    Structure Determination
    Method XRAY Chains 4
    Resolution (Å) 2.27 Rfree 0.21256
    Matthews' coefficent 3.38 Rfactor 0.17127
    Waters 529 Solvent Content 63.36

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    Ligand Information


    Google Scholar output for 1vm6
    1. Autoindexing with outlier rejection and identification of superimposed lattices
    NK Sauter, BK Poon - Journal of Applied Crystallography, 2010 - scripts.iucr.org
    2. Characterization of Dihydrodipicolinate Reductase from Thermotoga maritima Reveals Evolution of Substrate Binding Kinetics
    FG Pearce, C Sprissler, JA Gerrard - Journal of biochemistry, 2008 - Jpn Biochemical Soc
    3. The structure of dihydrodipicolinate reductase (DapB) from Mycobacterium tuberculosis in three crystal forms
    R Janowski, G Kefala, MS Weiss - Acta Crystallographica Section D: , 2009 - scripts.iucr.org
    4. Cloning, expression and crystallization of dihydrodipicolinate reductase from methicillin-resistant Staphylococcus aureus
    S Dommaraju, MA Gorman, C Dogovski - Section F: Structural , 2009 - scripts.iucr.org
    5. Catalytic mechanism and cofactor preference of dihydrodipicolinate reductase from methicillin-resistant Staphylococcus aureus
    SR Dommaraju, C Dogovski, PE Czabotar, L Hor - Archives of Biochemistry , 2011 - Elsevier
    6. Structure and nucleotide specificity of Staphylococcus aureus dihydrodipicolinate reductase (DapB)
    TS Girish, V Navratna, B Gopal - FEBS letters, 2011 - Elsevier
    7. Characterisation of the First Enzymes Committed to Lysine Biosynthesis in Arabidopsis thaliana
    MDW Griffin, JM Billakanti, A Wason, S Keller - PLoS One, 2012 - dx.plos.org
    8. RENNSH: A Novel alpha-Helix Identification Approach for Intermediate Resolution Electron Density Maps
    L Ma, M Reisert, H Burkhardt - IEEE/ACM Transactions on Computational , 2012 - dl.acm.org
    9. Comparative Structure and Function Analyses of Native and His-Tagged forms of Dihydrodipicolinate Reductase from Methicillin-Resistant Staphylococcus aureus
    C Dogovski, SR Dommaraju, LC Small - Protein Expression and , 2012 - Elsevier
    10. Molecular cloning, biochemical and biophysical studies of Dihydrodipicolinate reductase of Pseudomonas aeruginosa PAO1
    V Anand, A Gautam, D Sareen, TP Singh - Int. J. Integ. Biol, 2011 - ijib.classicrus.com

    Protein Summary

    The gene TM1520 from Thermotoga maritima encodes dihydrodipicolinate reductase from DapB superfamily PF01113 COG0289.  Both N-terminal DapB-N (NAD(P) binding domain) and C-terminal DapB-C domains are present in the structure.  Dihydrodipicolinate reductase is an enzyme, also found in higher plants, which is involved in the biosynthesis of diaminopimelic acid, a component of bacterial cell walls, and the essential amino acid L-lysine. It catalyses reduced pyridine nucleotide-dependent reduction of the alpha,beta-unsaturated cyclic imine, dihydrodipicolinate, to generate tetrahydrodipicolinate.  As this enzyme is not found in mammals it is a potential target for the development of novel antibacterial and herbicidal compounds.  The structures of the E.coli 1DIH and Mycobacterium tuberculosis  1P9L enzyme homologues have been determined.

    Ligand Summary





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