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1vpm

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

    Title Crystal structure of Acyl-CoA hydrolase (NP_241664.1) from Bacillus halodurans at 1.66 A resolution. To be published
    Site JCSG
    PDB Id 1vpm Target Id 356420
    Molecular Characteristics
    Source Bacillus halodurans c-125
    Alias Ids TPS1360,NP_241664.1 Molecular Weight 17326.78 Da.
    Residues 157 Isoelectric Point 6.92
    Sequence miqsypversrtiqtrlvlppdtnhlgtifggkvlayideiaaltamkhansavvtasidsvdfkssat vgdalelegfvthtgrtsmevyvrvhsnnlltgertlttesfltmvavdesgkpkpvpqvepqteeekr lyetaparkenrkkraalr
      BLAST   FFAS

    Structure Determination
    Method XRAY Chains 3
    Resolution (Å) 1.66 Rfree 0.19669
    Matthews' coefficent 2.40 Rfactor 0.17012
    Waters 310 Solvent Content 48.39

    Ligand Information
    Ligands
    Metals

    Jmol

     
    Google Scholar output for 1vpm
    1. The Buccaneer software for automated model building. 1. Tracing protein chains
    K Cowtan - Acta Crystallographica Section D: Biological , 2006 - scripts.iucr.org
     
    2. 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
     
    3. Structural basis for recruitment of tandem hotdog domains in acyl-CoA thioesterase 7 and its role in inflammation
    JK Forwood, AS Thakur, G Guncar - Proceedings of the , 2007 - National Acad Sciences
     
    4. Structure of YciA from Haemophilus influenzae (HI0827), a Hexameric Broad Specificity Acyl-Coenzyme A Thioesterase,
    MA Willis, Z Zhuang, F Song, A Howard - Biochemistry, 2008 - ACS Publications
     
    5. 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
     
    6. Structure and function of a Campylobacter jejuni thioesterase Cj0915, a hexameric hot dog fold enzyme
    T Yokoyama, KJ Choi, AM Bosch, HJ Yeo - Biochimica et Biophysica Acta ( , 2009 - Elsevier
     
    7. Ligand-induced conformational changes within a hexameric Acyl-CoA thioesterase
    M Marfori, B Kobe, JK Forwood - Journal of Biological Chemistry, 2011 - ASBMB
     
    8. Investigating diproline segments in proteins: Occurrences, conformation and classification
    I Saha, N Shamala - Biopolymers, 2012 - Wiley Online Library
     

    Protein Summary

    The gene NP_241664.1 from Bacillus halodurans encodes the enzyme acyl-CoA hydrolase EC:3.1.2.20, a member of 4HBT-like family, thioesterase superfamily PF03061.  The enzyme belongs to the class of alpha and beta (a+b) proteins and reveals Thioesterase/thiol ester dehydrase-isomerase fold type SCOP54636. The enzyme deacylates long-chain fatty acids by hydrolyzing acyl-CoA thioesters to free fatty acids and CoA-SH. Eukaryotic members of this family are expressed in brain, testis, and brown adipose tissues. The archeal and eukaryotic members of this family have two tandem copies of the conserved hot dog fold, while most bacterial members have only one copy.  The structure of the enzyme homologue from Bacillus cereus has been solved 1Y7U.

    Ligand Summary



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