.
The Open Protein Structure Annotation Network
PDB Keyword
.

1vm6

    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

    Pathway

    Reactions found in Metabolic Reconstruction for TM1520

    Name: dihydrodipicolinate reductase (NADH) reversible
    Metabolic Subsystem: Lysine Biosynthesis
    Reaction: : 23dhdp + h + nadh <==> nad + thdp
    Classification: EC:1.3.1.26
     

    Ligand Information
    Ligands
    Metals

    Jmol

     
    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



    References

    Reviews

    References

     

    No references found.

    Tag page

    Files (0)

     
    You must login to post a comment.
    All content on this site is licensed under a Creative Commons Attribution 3.0 License
    Powered by MindTouch