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1vme

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

    Title Crystal structure of Flavoprotein (TM0755) from Thermotoga maritima at 1.80 A resolution. To be published
    Site JCSG
    PDB Id 1vme Target Id 282625
    Molecular Characteristics
    Source Thermotoga maritima msb8
    Alias Ids TPS1232,TM0755, 29349534, 89997 Molecular Weight 45268.84 Da.
    Residues 398 Isoelectric Point 5.52
    Sequence mpkiwterifddpeiyvlridddriryfeavweipegisynaylvklnganvlidgwkgnyakefidal skivdpkeithiivnhtepdhsgslpatlktighdveiiasnfgkrllegfygikdvtvvkdgeereig gkkfkfvmtpwlhwpdtmvtyldgilfscdvgggyllpeilddsnesvverylphvtkyivtvighykn yilegaeklsslkikallpghgliwkkdpqrllnhyvsvakgdpkkgkvtviydsmygfvenvmkkaid slkekgftpvvykfsdeerpaiseilkdipdsealifgvstyeaeihplmrftlleiidkanyekpvlv fgvhgwapsaertagellketkfrilsfteikgsnmderkieeaisllkkele
      BLAST   FFAS

    Structure Determination
    Method XRAY Chains 2
    Resolution (Å) 1.80 Rfree 0.18104
    Matthews' coefficent 2.41 Rfactor 0.14687
    Waters 442 Solvent Content 48.58

    Ligand Information
    Ligands
    Metals

    Jmol

     
    Google Scholar output for 1vme
    1. The Buccaneer software for automated model building. 1. Tracing protein chains
    K Cowtan - Acta Crystallographica Section D: Biological , 2006 - scripts.iucr.org
     
    2. Three-dimensional structure of the quorum-quenching N-acyl homoserine lactone hydrolase from Bacillus thuringiensis
    D Liu, BW Lepore, GA Petsko - Proceedings of the , 2005 - National Acad Sciences
     
    3. Real-space protein-model completion: an inverse-kinematics approach
    H Van Den Bedem, I Lotan, JC Latombe - Section D: Biological , 2004 - scripts.iucr.org
     
    4. The hyperthermophilic anaerobe Thermotoga maritima is able to cope with limited amount of oxygen: insights into its defence strategies
    C Le Fourn, ML Fardeau, B Ollivier - Environmental , 2008 - Wiley Online Library
     
    5. Structural analysis of metal sites in proteins: non-heme iron sites as a case study
    C Andreini, I Bertini, G Cavallaro - Journal of molecular , 2009 - Elsevier
     
    6. Structural studies on flavodiiron proteins
    JB Vicente, MA Carrondo, M Teixeira, C Frazao - Methods in enzymology, 2008 - Elsevier
     
    7. Insights into the nitric oxide reductase mechanism of flavo-diiron proteins from flavin-free enzyme
    T Hayashi, JD Caranto, DA Wampler, DM Kurtz - Biochemistry, 2010 - ACS Publications
     
    8. Quaternary structure of flavorubredoxin as revealed by synchrotron radiation small-angle X-ray scattering
    MV Petoukhov, JB Vicente, PB Crowley, MA Carrondo - Structure, 2008 - Elsevier
     
    9. Flavodiiron proteins: nitric oxide and/or oxygen reductases
    JB Vicente, MA Carrondo, M Teixeira - of Inorganic and , 2007 - Wiley Online Library
     
    10. Dioxygen and nitric oxide pathways and affinity to the catalytic site of rubredoxin: oxygen oxidoreductase from Desulfovibrio gigas
    BL Victor, AM Baptista, CM Soares - Journal of Biological Inorganic , 2009 - Springer
     
    11. Crystal structure of TTHA1429, a novel metallo___lactamase superfamily protein from Thermus thermophilus HB8
    A Yamamura, J Ohtsuka, K Kubota - Proteins: Structure, , 2008 - Wiley Online Library
     
    12. Flavodiiron proteins and their role in cyanobacteria
    VL Gonalves, JB Vicente, LM Saraiva - Bioenergetic Processes , 2011 - Springer
     
    13. Modeling structural heterogeneity in proteins from X-ray data
    A Dhanik, H Van Den Bedem, A Deacon - Algorithmic Foundation of , 2009 - Springer
     
    14. http://3Dsig. weizmann. ac. il
    I An - 2006 - 3dsig.weizmann.ac.il
     

    Protein Summary


    The TM0755 gene from Thermotoga maritima codes for protein containing 2 easily distinguished domains.  The N-terminal domain belongs to the lactamase B superfamily (PF00753), while the C-terminal domain belongs to the FMN redox superfamily (PF00258).  The beta-lactamase domain has been reported for many proteins [Ref].  The crystal structure of highly homologous beta-lactamase from Bacillus cereus has been deposited 1BMC.  This type of beta-lactamases require Zn2+ ions for catalysis.  Although no Zn ions are found in the TMO755 structure, the proper spacing of histidine residues at positions 74, 79 and 84 indicates possible metal ion coordination site.  The flavoprotein domain of the TM0755 is a part of proteins that function in various electron transport systems.  The role of this domain in the context of beta-lactamase domain is unclear but genome context suggests a role in oxidative stress protection (high probability of functional association with rubredoxin, rubrerythrin, alkyl hydroperoxide reductase, superoxide reductase).

    Ligand Summary



    References

    Reviews

    References

     

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