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1o5h

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

    Title Crystal structure of a formiminotetrahydrofolate cyclodeaminase (TM1560) from Thermotoga maritima at 2.80 A resolution reveals a new fold. Proteins 58 976-981 2005
    Site JCSG
    PDB Id 1o5h Target Id 283417
    Molecular Characteristics
    Source Thermotoga maritima msb8
    Alias Ids TPS1299,TM1560, 84794 Molecular Weight 22712.09 Da.
    Residues 202 Isoelectric Point 4.96
    Sequence meverlslkefcdmvaerkptpgggavgsvvgamacalaemvanftrkkkgyedvepemeriveameea rlklfdlakkdmeafekvmkaykssegelqnalkeaasvpmdvirvmkdlaheleklaefgnknlasdt lnaadlchavfqvekvnvlinlkeisdetfrknmleeleeqeaqiegcyqrvkkmlegivwssk
      BLAST   FFAS

    Structure Determination
    Method XRAY Chains 2
    Resolution (Å) 2.80 Rfree 0.27814
    Matthews' coefficent 2.84 Rfactor 0.19927
    Waters Solvent Content 56.40

    Pathway

    Reactions found in Metabolic Reconstruction for TM1560

    Name: formimidoyltransferase cyclodeaminase reversible
    Metabolic Subsystem: Folate Metabolism
    Reaction: : 5forthf + h <==> methf + nh4
    Classification: EC:4.3.1.4
     

    Ligand Information
    Ligands
    Metals

    Jmol

     
    Google Scholar output for 1o5h
    1. Microbial biochemistry, physiology, and biotechnology of hyperthermophilic Thermotoga species
    SB Conners, EF Mongodin, MR Johnson - FEMS microbiology , 2006 - Wiley Online Library
     
    2. Structural characterization of proteins using residue environments
    SD Mooney, MHP Liang, R DeConde - PROTEINS: Structure, , 2005 - Wiley Online Library
     
    3. 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
     
    4. Short-Lived _-Helical Intermediates in the Folding of _-Sheet Proteins
    E Chen, ML Everett, ZE Holzknecht, RA Holzknecht - Biochemistry, 2010 - ACS Publications
     
    5. Crystal structure of a formiminotetrahydrofolate cyclodeaminase (TM1560) from Thermotoga maritima at 2.80 resolution reveals a new fold
    Q Xu, R Schwarzenbacher, D McMullan - Proteins: Structure, , 2005 - Wiley Online Library
     
    6. Carbohydrate utilization pathway analysis in the hyperthermophile Thermotoga maritima
    SB Conners - 2006 - repository.lib.ncsu.edu
     

    Protein Summary

    Formiminotetrahydrofolate cyclodeaminase (TM1560) from Thermotoga maritima (FTCD_CD, EC 4.3.1.4; COG3404, pfam04961) is involved in folate metabolism (PubMed:15651027).

    TM1560 is similar to protein domain of bifunctional, Golgi-associated formiminotransferase cyclodeaminase (PDB id: 1tt9) - a mammalian protein that plays important roles in coupling histidine catabolism with folate metabolism and integrating the Golgi complex with the vimentin intermediate filament cytoskeleton (PubMed:15272307).

    TM1560 has methenyltetrahydrofolate cyclohydrolase-like fold (SCOP sunid:101261) - closed 5 helical bundle with left-handed twist.

    Ligand Summary



    References

    Reviews

    References

     

    No references found.

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