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2gvk

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

    Title Crystal structures of two novel dye-decolorizing peroxidases reveal a beta-barrel fold with a conserved heme-binding motif. Proteins 69 223-233 2007
    Site JCSG
    PDB Id 2gvk Target Id 361324
    Molecular Characteristics
    Source Bacteroides thetaiotaomicron vpi-5482
    Alias Ids TPS1468,NP_810132.1, PF04261, 423540 Molecular Weight 35025.62 Da.
    Residues 316 Isoelectric Point 4.90
    Sequence mnpfqnsfgghipqdvagkqgenvifivynltdspdtvdkvkdvcanfsamirsmrnrfpdmqfsctmg fgadawtrlfpdkgkpkelstfseikgekytavstpgdllfhirakqmglcfefasildeklkgavvsv dethgfrymdgkaiigfvdgtenpavdenpyhfavigeedadfaggsyvfvqkyihdmvawnalpveqq ekvigrhkfndvelsdeekpgnahnavtnigddlkivranmpfantskgeygtyfigyastfsttrrml enmfigspagntdrlldfstaitgtlffvpsydllgelge
      BLAST   FFAS

    Structure Determination
    Method XRAY Chains 1
    Resolution (Å) 1.60 Rfree 0.19
    Matthews' coefficent 2.98 Rfactor 0.164
    Waters 327 Solvent Content 58.78

    Ligand Information
    Ligands
    Metals

    Jmol

     
    Google Scholar output for 2gvk
    1. DyP-type peroxidases comprise a novel heme peroxidase family
    Y Sugano - Cellular and molecular life sciences, 2009 - Springer
     
    2. DyP, a unique dye-decolorizing peroxidase, represents a novel heme peroxidase family
    Y Sugano, R Muramatsu, A Ichiyanagi, T Sato - Journal of Biological , 2007 - ASBMB
     
    3. Structural basis of enzyme encapsulation into a bacterial nanocompartment
    M Sutter, D Boehringer, S Gutmann - Nature structural & , 2008 - nature.com
     
    4. Crystal structures of two novel dye_decolorizing peroxidases reveal a __barrel fold with a conserved heme_binding motif
    C Zubieta, S Krishna, M Kapoor - Proteins: Structure, , 2007 - Wiley Online Library
     
    5. Identification and structural characterization of heme binding in a novel dye_decolorizing peroxidase, TyrA
    C Zubieta, R Joseph, S Sri Krishna - Proteins: Structure, , 2007 - Wiley Online Library
     
    6. Identification of DypB from Rhodococcus jostii RHA1 as a Lignin Peroxidase
    M Ahmad, JN Roberts, EM Hardiman, R Singh - Biochemistry, 2011 - ACS Publications
     
    7. Characterization of DyP Peroxidases from Rhodococcus jostii RHA1
    JN Roberts, R Singh, JC Grigg, MEP Murphy - Biochemistry, 2011 - ACS Publications
     
    8. Analysis of in vitro bioactivity data extracted from drug discovery literature and patents: Ranking 1654 human protein targets by assayed compounds and molecular
    C Southan, K Boppana, SARP Jagarlapudi - Journal of , 2011 - Springer
     
    9. Ligands in crystal structures that aid in functional characterization
    AE Speers, BF Cravatt - Acta Crystallographica Section F: Structural , 2010 - scripts.iucr.org
     
    10. Protein structural classification and family identification by multifractal analysis and wavelet spectrum
    SM Zhu, ZG Yu, A Vo - Chinese Physics B, 2011 - iopscience.iop.org
     
    11. The catalytic mechanism of dye_decolorizing peroxidase DyP may require the swinging movement of an aspartic acid residue
    T Yoshida, H Tsuge, H Konno, T Hisabori - FEBS , 2011 - Wiley Online Library
     
    12. Identification and Molecular Characterization of a Novel DyP-Type Peroxidase from Pseudomonas aeruginosa PKE117
    J Li, C Liu, BZ Li, HL Yuan, JS Yang - Applied biochemistry and , 2012 - Springer
     

    Protein Summary

    BtDyP from Bacteroides thetaiotaomicron descr (strain VPI-5482) is a Dye-decolorizing peroxidase (DyP), a member of a new family of heme-dependent peroxidases recently identified in fungi and bacteria.

    Ligand Summary



    References

    Reviews

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