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

    Title Functional and structural characterization of a thermostable acetyl esterase from Thermotoga maritima. Proteins 80 1545-1559 2012
    Site JCSG
    PDB Id 1vlq Target Id 281958
    Related PDB Ids 3m82 3m83 3m81 
    Molecular Characteristics
    Source Thermotoga maritima msb8
    Alias Ids TPS1182,TM0077, 83900 Molecular Weight 37154.48 Da.
    Residues 325 Isoelectric Point 5.80
    Sequence maffdlpleelkkyrperyeekdfdefweetlaesekfpldpvfermeshlktveaydvtfsgyrgqri kgwllvpkleeeklpcvvqyigynggrgfphdwlfwpsmgyicfvmdtrgqgsgwlkgdtpdypegpvd pqypgfmtrgildprtyyyrrvftdavraveaaasfpqvdqeriviaggsqgggialavsalskkakal lcdvpflchfrravqlvdthpyaeitnflkthrdkeeivfrtlsyfdgvnfaarakipalfsvglmdni cppstvfaaynyyagpkeiriypynnhegggsfqaveqvkflkklfekg
      BLAST   FFAS

    Structure Determination
    Method XRAY Chains 12
    Resolution (Å) 2.10 Rfree 0.22336
    Matthews' coefficent 2.93 Rfactor 0.18354
    Waters 2464 Solvent Content 57.69

    Ligand Information


    Google Scholar output for 1vlq
    1. N-terminal domain of _B-crystallin provides a conformational switch for multimerization and structural heterogeneity
    S Jehle, BS Vollmar, B Bardiaux - Proceedings of the , 2011 - National Acad Sciences
    2. Application of a sensitive collection heuristic for very large protein families: evolutionary relationship between adipose triglyceride lipase (ATGL) and classic
    G Schneider, G Neuberger, M Wildpaner - BMC , 2006 - biomedcentral.com
    3. Carboxylic ester hydrolases from hyperthermophiles
    M Levisson, J Van Der Oost, SWM Kengen - Extremophiles, 2009 - Springer
    4. Structural and functional characterization of a promiscuous feruloyl esterase (Est1E) from the rumen bacterium Butyrivibrio proteoclasticus
    DC Goldstone, SG Villas_Bas, M Till - Proteins: Structure, , 2010 - Wiley Online Library
    5. Neisseria gonorrheae O-acetylpeptidoglycan esterase, a serine esterase with a Ser-His-Asp catalytic triad
    JT Weadge, AJ Clarke - Biochemistry, 2007 - ACS Publications
    6. Functional and structural characterization of a thermostable acetyl esterase from Thermotoga maritima
    M Levisson, G Won Han, MC Deller - Proteins: Structure, , 2012 - Wiley Online Library
    7. The structural basis for the narrow substrate specificity of an acetyl esterase from Thermotoga maritima
    MK Hedge, AM Gehring, CT Adkins, LA Weston - et Biophysica Acta (BBA , 2012 - Elsevier
    8. Hyperthermostable acetyl xylan esterase
    K Drzewiecki, A Angelov, M Ballschmiter - Microbial , 2010 - Wiley Online Library
    9. Computational investigations of enzyme catalysis, design, and conformational aspects of drug-target interactions
    AJT Smith - 2008 - books.google.com
    10. Integrating sequence and structure data for identifying functional sites on protein structures
    MHP Liang - 2005 - bmir.stanford.edu
    R Dicosimo, MS Payne, T Yin - US Patent 20,120,016,025, 2012 - freepatentsonline.com

    Protein Summary

    The TM0077 gene of Thermotoga maritima encodes an acetyl xylan esterase (AXE) (EC, PF05448, NP_227893), a deacetylase of xylan, a major component of lignocellulose, and xylo-oligosaccharides. The structure (1vlq) forms a single three-layered a/b/a domain that belongs to the alpha/beta hydrolase fold shared by cephalosporin C deacetylases (CAHs) (EC (PDB id: 1ods, 1l7a), enzymes that hydrolyse the acetyl ester bond on the 10-position of the antibiotic cephalosporin C. The two enzymes have identical tertiary (main chain rmsd 1.3 Å over 325 residues, 40% sequence identity) and quaternary structures (dimer of trimers). DALI top hits are with CAHs like 1ods  and 1l7a (Z=46), and with AXEs like 3fyu and 3fcy (Z=45); a weaker hit (Z=23) is observed with 2hu7, an acylamino acid releasing enzyme.


    It has been suggested that AXEs and CAHs 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 AXEs and CAHs 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





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