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1vr3

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

    Title Crystal structure of acireductone dioxygenase (ARD) from Mus musculus at 2.06 angstrom resolution. Proteins 64 808-813 2006
    Site JCSG
    PDB Id 1vr3 Target Id 354741
    Molecular Characteristics
    Source Mus musculus
    Alias Ids TPS1340,13543033, 2.60.120.10, 89589, 289614, 289622, 89750, 289478, 90014, 289344, 289410, 89807 Molecular Weight 21522.48 Da.
    Residues 179 Isoelectric Point 5.31
    Sequence mvqawymdestadprkphraqpdrpvsleqlrtlgvlywkldadkyendpelekirkmrnyswmdiiti ckdtlpnyeekikmffeehlhldeeiryilegsgyfdvrdkedkwirismekgdmitlpagiyhrftld eknyvkamrlfvgepvwtpynrpadhfdarvqymsflegta
      BLAST   FFAS

    Structure Determination
    Method XRAY Chains 1
    Resolution (Å) 2.06 Rfree 0.19532
    Matthews' coefficent 3.71 Rfactor 0.16229
    Waters 169 Solvent Content 66.57

    Ligand Information
    Ligands
    Metals

    Jmol

     
    Google Scholar output for 1vr3
    1. Structural studies on 2-oxoglutarate oxygenases and related double-stranded _-helix fold proteins
    IJ Clifton, MA McDonough, D Ehrismann - Journal of inorganic , 2006 - Elsevier
     
    2. The Buccaneer software for automated model building. 1. Tracing protein chains
    K Cowtan - Acta Crystallographica Section D: Biological , 2006 - scripts.iucr.org
     
    3. Structure and mechanism of mouse cysteine dioxygenase
    JG McCoy, LJ Bailey, E Bitto - Proceedings of the , 2006 - National Acad Sciences
     
    4. Variations of the 2_His_1_carboxylate Theme in Mononuclear Non_Heme FeII Oxygenases
    GD Straganz, B Nidetzky - ChemBioChem, 2006 - Wiley Online Library
     
    5. Decision-making in structure solution using Bayesian estimates of map quality: the PHENIX AutoSol wizard
    TC Terwilliger, PD Adams, RJ Read - Section D: Biological , 2009 - scripts.iucr.org
     
    6. A refined model for the structure of acireductone dioxygenase from Klebsiella ATCC 8724 incorporating residual dipolar couplings
    TC Pochapsky, SS Pochapsky, T Ju, C Hoefler - Journal of biomolecular , 2006 - Springer
     
    7. One protein, two enzymes revisited: A structural entropy switch interconverts the two isoforms of acireductone dioxygenase
    T Ju, RB Goldsmith, SC Chai, MJ Maroney - Journal of molecular , 2006 - Elsevier
     
    8. Crystal structure of acireductone dioxygenase (ARD) from Mus musculus at 2.06 resolution
    Q Xu, R Schwarzenbacher, S Sri Krishna - Proteins: Structure, , 2006 - Wiley Online Library
     
    9. Characterization of metal binding in the active sites of acireductone dioxygenase isoforms from Klebsiella ATCC 8724
    SC Chai, T Ju, M Dang, RB Goldsmith, MJ Maroney - Biochemistry, 2008 - ACS Publications
     
    10. A Trinuclear Nickel (II) Enediolate Complex: Synthesis, Characterization, and O2 Reactivity
    K Rudzka, AM Arif, LM Berreau - Inorganic chemistry, 2008 - ACS Publications
     
    11. ACIREDUCTONE DIOXYGENASE 1 (ARD1) is an effector of the heterotrimeric G protein _ subunit in Arabidopsis
    EJ Friedman, HX Wang, K Jiang, I Perovic - Journal of Biological , 2011 - ASBMB
     
    12. Nickel in Acireductone Dioxygenase
    TC Pochapsky, T Ju, M Dang - Nickel and Its , 2007 - Wiley Online Library
     
    13. Structure and Function of Atypically Coordinated Enzymatic Mononuclear Non-heme-Fe (II) Centers
    D Buongiorno, G Straganz - Coordination Chemistry Reviews, 2012 - Elsevier
     
    14. Synthetic Complexes of Relevance to Ni (II)-Containing Enzymes
    K Rudzka - 2008 - digitalcommons.usu.edu
     

    Protein Summary

    Mouse enzyme aci-reductone dioxygenase (ARD; GI: 13543033, EC 1.13.11.-, Pfam03079), belongs to the superfamily of metal-containing RmlC-like cupins (PubMed:16783794). ARD represents a branch point in the methionine salvage pathway leading from 5-methylthioadenosine (MTA) to methionine and catalyzes different reactions, depending on the type of metal ion bound in the active site (PubMed:11371200, 9880484).

    Proteins from this family, such as immediate-early ethylene response gene OsARD1 (PubMed:16297065) were proposed to be part of early feedback activation of the methionine cycle by low levels of ethylene  to ensures the high and continuous rates of ethylene synthesis required for long-term ethylene-mediated submergence adaptation without depleting the tissue of AdoMet. OsARD was also found to be novel water-deficit-suppressed gene (PMID: 16169685). Another member of ARD family - membrane-type 1 matrix metalloproteinase cytoplasmic tail binding protein-1 (MTCBP-1) acts as an eukaryotic aci-reductone dioxygenase (ARD) in the methionine salvage pathway (PMID: 15938715) and is possible multifunctional protein acting as an invasion suppressor down-regulated in tumors (PubMed:14718544). Protein Sip-L (from ARD protein family) was identified as cellular factors that was capable of supporting hepatitis C virus replication in 293EBNA cells (PMID: 11602742). The mRNA of another protein (GenBank:AAC08430, gi2996183) from ARD protein family is abundant in the third stage larvae of the parasitic nematode, Ostertagia ostertagi (PubMed:10769181).

    ARD structure is typified by two antiparallel beta-sheets that form a cup-shaped, beta-sandwich jelly roll and has structure similar to RmlC-like cupins superfamily.

    Ligand Summary



    References

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