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1l7a

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

    Title 1.5A crystal structure of the Cephalosporin C deacetylase. To be Published
    Site MCSG
    PDB Id 1l7a Target Id
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    Molecular Characteristics
    Source
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    Alias Ids
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    TPS4487,P94388, 1423
    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 2
    Resolution (Å)
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    Rfree
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    Matthews' coefficent 2.16 Rfactor 0.185
    Waters
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    Solvent Content 43.09

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    Ligand Information
    Ligands
    Metals

    Jmol

     
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    Google Scholar output for 1l7a
    1. Assessment of homology_based predictions in CASP5
    A Tramontano, V Morea - Proteins: Structure, Function, and , 2003 - Wiley Online Library
     
    2. Finding functional sites in structural genomics proteins
    A Stark, A Shkumatov, RB Russell - Structure, 2004 - Elsevier
     
    3. Are structural biases at protein termini a signature of vectorial folding?
    A Laio, C Micheletti - PROTEINS: Structure, Function, and , 2006 - Wiley Online Library
     
    4. Structural classification by the Lipase Engineering Database: a case study of Candida antarctica lipase A
    M Widmann, PB Juhl, J Pleiss - BMC genomics, 2010 - biomedcentral.com
     
    5. A fold-recognition approach to loop modeling
    C Levefelt, D Lundh - Journal of molecular modeling, 2006 - Springer
     
    6. Recognition of Interaction Interface Residues in Low-Resolution Structures of Protein Assemblies Solely from the Positions of C_ Atoms
    RA Gadkari, D Varughese, N Srinivasan - PloS one, 2009 - dx.plos.org
     
    7. A novel structural motif and structural trees for proteins containing it
    AM Kargatov, AV Efimov - Biochemistry (Moscow), 2010 - Springer
     
    8. Stochastic pairwise alignments and scoring methods for comparative protein structure modeling
    AC Marko, K Stafford, T Wymore - Journal of chemical information , 2007 - ACS Publications
     
    9. Topologies of surfaces on molecules and their computation in O (n) time
    DS Kim, Y Cho, J Ryu, CM Kim - Computer-Aided Design, 2010 - Elsevier
     
    10. Synthesis of functionalized furopyrazines as restricted dipeptidomimetics
    S Claerhout, S Sharma, C Skld, C Cavaluzzo - Tetrahedron, 2012 - Elsevier
     
    11. Protein Structure Prediction Using an Augmented Homology Modeling Method: Key Importance of Iterative-Procedures for Obtaining Consistent Quality Models
    S McDonald, S Mylvaganam - Current , 2005 - ingentaconnect.com
     
    12. Computational and experimental investigations of forces in protein folding
    DA Schell - 2003 - txspace.di.tamu.edu
     
    13. Hyperthermostable acetyl xylan esterase
    K Drzewiecki, A Angelov, M Ballschmiter - Microbial , 2010 - Wiley Online Library
     
    14. Dead_End elimination with perturbations (DEEPer): A provable protein design algorithm with continuous sidechain and backbone flexibility
    MA Hallen, DA Keedy - : Structure, Function, and , 2012 - Wiley Online Library
     
    15. Computational investigations of enzyme catalysis, design, and conformational aspects of drug-target interactions
    AJT Smith - 2008 - books.google.com
     
    16. Integrating sequence and structure data for identifying functional sites on protein structures
    MHP Liang - 2005 - bmir.stanford.edu
     

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    Protein Summary

    The cah gene of Bacillus subtilis encodes a cephalosporin C deacetylase (CAH) (EC 3.1.1.41), an enzyme that hydrolyses the acetyl ester bond on the 10-position of the antibiotic cephalosporin C. The structure forms a single three-layered a/b/a domain that belongs to the alpha/beta hydrolase fold shared by acetyl xylan esterases (AXEs) (EC 3.1.1.72, PF05448) (PDB id: 1vlq), enzymes that deacetylase xylan, a major component of lignocellulose, and xylo-oligosaccharides. The two enzymes have identical tertiary (main chain rmsd 1.3 Å over 325 residues, 40% sequence identity) and quaternary structures (dimer of trimers).


    It has been suggested that CAHs and AXEs represent a single class of proteins exhibiting a multifunctional deacetylase activity against a range of small substrates (Vincent 2003). By analogy with self-compartentalising proteases, oligomerization of CAHs and AXEs has been proposed to shield their active sites with a narrow tunnel leading to the center of the molecule and the six active-center catalytic triads pointing towards the tunnel interior, thus sequestered away from cytoplasmic contents (Vincent 2003).

    Ligand Summary

    Reviews

    References

     

    No references found.

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