The Open Protein Structure Annotation Network
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    Table of contents
    1. 1. Protein Summary
    2. 2. Ligand Summary
    3. 3. References

    Title Crystal structure of Transaldolase (EC (TM0295) from Thermotoga maritima at 2.40 A resolution. To be published
    Site JCSG
    PDB Id 1vpx Target Id 282171
    Molecular Characteristics
    Source Thermotoga maritima msb8
    Alias Ids TPS1198,TM0295, 282153 Molecular Weight 24212.00 Da.
    Residues 218 Isoelectric Point 5.14
    Sequence mkifldtanleeikkgvewgivdgvttnptliskegaefkqrvkeicdlvkgpvsaevvsldyegmvre arelaqiseyvvikipmtpdgikavktlsaegiktnvtlvfspaqailaakagatyvspfvgrmddlsn dgmrmlgeiveiynnygfeteiiaasirhpmhvveaalmgvdivtmpfavleklfkhpmtdlgierfme dwkkylenlkk
      BLAST   FFAS

    Structure Determination
    Method XRAY Chains 20
    Resolution (Å) 2.40 Rfree 0.24694
    Matthews' coefficent 2.75 Rfactor 0.19632
    Waters 103 Solvent Content 54.87

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    Ligand Information


    Google Scholar output for 1vpx
    1. Microbial biochemistry, physiology, and biotechnology of hyperthermophilic Thermotoga species
    SB Conners, EF Mongodin, MR Johnson - FEMS microbiology , 2006 - Wiley Online Library
    2. The JCSG MR pipeline: optimized alignments, multiple models and parallel searches
    R Schwarzenbacher, A Godzik - Section D: Biological , 2007 - scripts.iucr.org
    3. Phage auxiliary metabolic genes and the redirection of cyanobacterial host carbon metabolism
    LR Thompson, Q Zeng, L Kelly - Proceedings of the , 2011 - National Acad Sciences
    4. The Transaldolase Family: New Synthetic Opportunities from an Ancient Enzyme Scaffold
    AK Samland, M Rale, GA Sprenger - ChemBioChem, 2011 - Wiley Online Library
    5. A thermostable recombinant transaldolase with high activity over a broad pH range
    SY Huang, YHP Zhang, JJ Zhong - Applied Microbiology and , 2012 - Springer
    6. Computational methods for functional site identification suggest a substrate access channel in transaldolase
    M Silberstein, MR Landon, YE Wang, A Perl - GENOME INFORMATICS , 2006 - jsbi.org
    7. Carbohydrate utilization pathway analysis in the hyperthermophile Thermotoga maritima
    SB Conners - 2006 - repository.lib.ncsu.edu
    8. Conservation of structure and mechanism within the transaldolase enzyme family
    AK Samland, S Baier, M Schrmann, T Inoue - FEBS , 2012 - Wiley Online Library

    Protein Summary

    The TM0295 gene of Thermotoga maritima encodes a transaldolase (PF00923, COG0176, EC, an enzyme involved in the non-oxidative phase of the pentose pathway and the generation of NADP. TM0295 folds into a TIM beta/alpha barrel and is very similar to the transaldolase from another hyperthermophile, Thermus thermophilus (PDB id: 1wx0) with a main-chain rmsd of 0.7 Å over 191 residues and 58% sequence identity. Significant structural similarity is also observed with the fructose-6-phosphate aldolase (FSA) from Escherichia coli (PDB id: 1l6w, main-chain rmsd 1.4 Å over 202 residues, 32% sequence identity), a member of the class I aldolases that can catalyse exclusively either a simple aldol cleavage/condensation reaction or a transfer reaction (Thorell 2002). Like the E. coli FSA, TM0295 adopts a decameric quaternary structure with two ring-like pentamers packing like a doughnut with subunit swapping of the C-terminal helix acting as a major determinant in pentamer formation (Thorell 2002).


    Structural superimposition of TM0295 with the FSA from E. coli shows that in addition to overall structural similarity, the catalytic lysine (Lys83 in TM0295) is also conserved. TM0295 has been shown to function exclusively as a transaldolase with no FSA activity (Shurmann 2001). The switch between transaldolase and aldolase activities observed in the E. coli FSA could be achieved by control of the relative stability of the Schiff base intermediate of the and/or modification of the affinity of the acceptor substrate (Thorell 2002).

    Ligand Summary





    No references found.

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