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1j6r

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

    Title Crystal structure of Activation (AdoMet binding) domain of Methionine synthase (TM0269) from Thermotoga maritima at 2.2 A resolution. To be published
    Site JCSG
    PDB Id 1j6r Target Id 282146
    Molecular Characteristics
    Source Thermotoga maritima msb8
    Alias Ids TPS1196,TM0269, 84849, 89350 Molecular Weight 22889.11 Da.
    Residues 202 Isoelectric Point 5.13
    Sequence mpkveiapseikipdnvlkaklgfggaeeipeefrktvnrayeelldaakpvvlwrdfevdgslsfddm rltgelatkhlsgskiitvflatlgkkvdekieeyfrkgedllaffidgiasemveyalrkvdaelrmk rsnlegsfrispgygdlplslnkkiaeifkeevdvnviedsyvlvprktitafvgwreknekqt
      BLAST   FFAS

    Structure Determination
    Method XRAY Chains 2
    Resolution (Å) 2.30 Rfree 0.29
    Matthews' coefficent 2.99 Rfactor 0.251
    Waters 103 Solvent Content 58.81

    Pathway

    Reactions found in Metabolic Reconstruction for TM0269

    Name: methionine synthase
    Other genes that carryout this rxn: TM0268
    Metabolic Subsystem: Methionine Metabolism
    Reaction: : 5mthf + hcys-L --> h + met-L + thf
    Classification: EC:2.1.1.13
     

    Ligand Information
    Ligands
    Metals

    Jmol

     
    Google Scholar output for 1j6r
    1. Structures of the N-terminal modules imply large domain motions during catalysis by methionine synthase
    JC Evans, DP Huddler, MT Hilgers - Proceedings of the , 2004 - National Acad Sciences
     
    2. Structural characterization of proteins using residue environments
    SD Mooney, MHP Liang, R DeConde - PROTEINS: Structure, , 2005 - Wiley Online Library
     
    3. Active site identification through geometry-based and sequence profile-based calculations: burial of catalytic clefts
    R Greaves, J Warwicker - Journal of molecular biology, 2005 - Elsevier
     
    4. Shotgun crystallization strategy for structural genomics II: crystallization conditions that produce high resolution structures for T. maritima proteins
    R Page, AM Deacon, SA Lesley - Journal of structural and , 2005 - Springer
     
    5. Efficient recognition of protein fold at low sequence identity by conservative application of Psi_BLAST: validation
    FJ Stevens - Journal of Molecular Recognition, 2005 - Wiley Online Library
     
    6. The ether-cleaving methyltransferase system of the strict anaerobe Acetobacterium dehalogenans: analysis and expression of the encoding genes
    A Schilhabel, S Studenik, M Vdisch - Journal of , 2009 - Am Soc Microbiol
     
    7. Reactivation of methionine synthase from Thermotoga maritima (TM0268) requires the downstream gene product TM0269
    S Huang, G Romanchuk, K Pattridge, SA Lesley - Protein , 2007 - Wiley Online Library
     
    8. 1 Protein methyltransferases: Their distribution among the five structural classes of adomet-dependent methyltransferases
    HL Schubert, RM Blumenthal, X Cheng - The Enzymes, 2006 - Elsevier
     
    9. Of sequence and structure: Strategies of protein thermostability in evolutionary perspective
    IN Berezovsky, EI Shakhnovich - Arxiv preprint q-bio/0408007, 2004 - arxiv.org
     
    10. INAUGURAL ARTICLE by a Recently Elected Academy Member: Structures of the N-terminal modules imply large domain motions during catalysis by
    JC Evans, DP Huddler, MT Hilgers - Proceedings of the , 2004 - ncbi.nlm.nih.gov
     

    Protein Summary

    The TM0269 gene from Thermotoga maritima encodes the activation domain of a vitamin B12-dependent methionine synthase (PFAM:PF02965, GO:0008705). The structure adopts a methionine synthase activation domain-like fold

     

    Ligand Summary



    References

    Reviews

    References

     

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