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2qez

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

    Title Crystal structure of ethanolamine ammonia-lyase heavy chain (YP_013784.1) from Listeria monocytogenes 4b F2365 at 2.15 A resolution. To be published
    Site JCSG
    PDB Id 2qez Target Id 366145
    Molecular Characteristics
    Source Listeria monocytogenes str. 4b f2365
    Alias Ids TPS1472,YP_013784.1, PF06751, 90238 Molecular Weight 49863.95 Da.
    Residues 454 Isoelectric Point 5.20
    Sequence milktnlfghtyqfksitdvlakaneeksgdrlagvaaesaeervaakvvlskmtlgdlrnnpvvpyet devtriiqdqvndrihdsiknwtveelrewildhkttdadikrvargltseiiaavtklmsnldliyga kkirviahanttiglpgtfsarlqpnhptddpdgilaslmegltygigdaviglnpvddstdsvvrlln kfeefrskwdvptqtcvlahvktqmeamrrgaptglvfqsiagsekgntafgfdgatieearqlalqsg aatgpnvmyfetgqgselssdahfgvdqvtmearcygfakkfdpflvntvvgfigpeylydskqvirag ledhfmgkltgismgcdvcytnhmkadqndvenlsvlltaagcnfimgiphgddvmlnyqttgyhetat lrelfglkpikefdqwmekmgfsengkltsragdasiflk
      BLAST   FFAS

    Structure Determination
    Method XRAY Chains 6
    Resolution (Å) 2.15 Rfree 0.279
    Matthews' coefficent 2.28 Rfactor 0.228
    Waters 754 Solvent Content 46.12

    Ligand Information
    Ligands
    Metals

    Jmol

     
    Google Scholar output for 2qez
    1. PSI-2: structural genomics to cover protein domain family space
    BH Dessailly, R Nair, L Jaroszewski, JE Fajardo - Structure, 2009 - Elsevier
     
    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. Crystal structure of the EutL shell protein of the ethanolamine ammonia lyase microcompartment
    M Sagermann, A Ohtaki - Proceedings of the , 2009 - National Acad Sciences
     
    4. Critical Role of Arginine 160 of the EutB Protein Subunit for Active Site Structure and Radical Catalysis in Coenzyme B12-Dependent Ethanolamine Ammonia-lyase
    L Sun, OA Groover, JM Canfield, K Warncke - Biochemistry, 2008 - ACS Publications
     
    5. Comparative genomics of ethanolamine utilization
    O Tsoy, D Ravcheev, A Mushegian - Journal of bacteriology, 2009 - Am Soc Microbiol
     
    6. Purification and some properties of wild-type and N-terminal-truncated ethanolamine ammonia-lyase of Escherichia coli
    K Akita, N Hieda, N Baba, S Kawaguchi - Journal of , 2010 - Jpn Biochemical Soc
     
    7. Expression, crystallization and preliminary X-ray crystallographic study of ethanolamine ammonia-lyase from Escherichia coli
    N Shibata, H Tamagaki, S Ohtsuki, N Hieda - Section F: Structural , 2010 - scripts.iucr.org
     
    8. Multidisciplinary Assessments of the Structure and Function of Co-enzyme B12-Dependent Enzyme Ethanolamine Ammonia-lyase
    L Sun - 2009 - etd.library.emory.edu
     

    Protein Summary

    The gene LMOf2365_1185 (also known as eutB) from Listeria monocytogenes 4b f2365 encodes ethanolamine ammonia-lyase large (alpha) subunit (EutB) PF06751 COG4303.  The protein belongs to the class of alpha and beta (a+b) proteins and adopts a TIM beta/alpha-barrel fold type SCOP51350.  Ethanolamine ammonia-lyase (alternative name: ethanolamine deaminase) EC:4.3.1.7 is the enzyme which catalyzes the following reaction: ethanolamine <=> acetaldehyde + NH(3).  It requires cobalamin as a cofactor.  The enzyme enables bacteria to survive on small organic molecules such as ethanolamine as the sole source for carbon and nitrogen. 

    Ligand Summary



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