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The Open Protein Structure Annotation Network
PDB Keyword
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2hbo

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

    Title Crystal structure of hypothetical protein (np_422103.1) from Caulobacter crescentus at 1.85 A resolution. To be published
    Site JCSG
    PDB Id 2hbo Target Id
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    Molecular Characteristics
    Source
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    Alias Ids
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    TPS1481,NP_422103.1, 382773
    Molecular Weight
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    Da.
    Residues
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    Isoelectric Point
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    Sequence
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      BLAST   FFAS

    Structure Determination
    Method XRAY
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    Chains 1
    Resolution (Å)
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    Rfree
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    Matthews' coefficent 2.10 Rfactor 0.208
    Waters
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    Solvent Content 41.08

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    Ligand Information
    Ligands
    Metals

    Jmol

     
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    Google Scholar output for 2hbo
    1. Protein fold and structure in the truncated (2/2) globin family
    M Nardini, A Pesce, M Milani, M Bolognesi - Gene, 2007 - Elsevier
     
    2. Protein structure in the truncated (2/2) hemoglobin family
    A Pesce, M Nardini, M Milani, M Bolognesi - IUBMB life, 2007 - Wiley Online Library
     
    3. Analysis of proteins with the'hot dog'fold: Prediction of function and identification of catalytic residues of hypothetical proteins
    LS Pidugu, K Maity, K Ramaswamy - BMC structural , 2009 - biomedcentral.com
     
    4. Ab initio protein structure prediction with force field parameters derived from water_phase quantum chemical calculation
    D Katagiri, H Fuji, S Neya - Journal of computational , 2008 - Wiley Online Library
     
    5. Reconstruction of Protein Backbone with the alpha-Carbon Coordinates
    JH Wang, CB Yang, CT Tseng - Journal of Information Science , 2010 - etd.lib.nsysu.edu.tw
     
    6. The peculiar heme pocket of the 2/2 hemoglobin of cold-adapted Pseudoalteromonas haloplanktis TAC125
    BD Howes, D Giordano, L Boechi, R Russo - Journal of Biological , 2011 - Springer
     
    7. Structural characterization of a group II 2/2 hemoglobin from the plant pathogen Agrobacterium tumefaciens
    A Pesce, M Nardini, M LaBarre, C Richard - et Biophysica Acta (BBA , 2011 - Elsevier
     
    8. Reconstruction of Protein Backbone with the a-Carbon Coordinates
    JH Wang, CB Yang, CT Tseng - 2007 - asiair.asia.edu.tw
     
    9. Refinement of All-atom Backbone Prediction of Proteins
    HY Chang - 2008 - etd.lib.nsysu.edu.tw
     
    10. Structure and function of hemoproteins from cold-adapted organism
    R Russo - 2011 - fedoa.unina.it
     
    11. The truncated hemoglobin from Thermobifida fusca
    FP Nicoletti - Resonance Raman Spectroscopy As a Tool To Study , 2010 - unifi.it
     
    12. Structural and functional studies of hemoproteins from polar marine organisms
    D Coppola - 2011 - fedoa.unina.it
     

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    Protein Summary

    The gene CC_3309 from Caulobacter crescentus encodes the NP_422103 protein, a putative PaaI thioesterase (phenylacetic acid degradation protein), and a member of the thioesterase superfamily PF03061. Genome context analysis shows a predicted functional link (score 0.89) with CC_3308, a putative hydrolase.

    The enzyme belongs to the class of alpha and beta (a+b) proteins and adopts a  thioesterase/thiol ester dehydrase-isomerase (hot-dog) fold type SCOP54636. A DALI structural similarity search reports as top hits the thioesterase

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    (Z=16), the phenylacetic acid degradation protein PaaI
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    (Z=15), and the hypothetical protein PA5202 
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    (Z=15). The structures of the enzyme homologues from other organisms have been determined:
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      (Z=14), E. coli;
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    (Z=14), Thermus thermophilus.

    The enzyme participates in the aerobic phenylacetate degradation pathway.  This pathway targets a variety of environmental aromatics of natural and synthetic origin.  The enzyme is potentially useful for bioremediation of environmental aromatic pollutants and for chemical synthesis [Ref].  

    Ligand Summary



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