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1o4u

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

    Title Crystal structure of a type II quinolic acid phosphoribosyltransferase (TM1645) from Thermotoga maritima at 2.50 A resolution. Proteins 55 768-771 2004
    Site JCSG
    PDB Id 1o4u Target Id
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    Molecular Characteristics
    Source
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    Alias Ids
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    TPS1308,TM1645, 85077
    Molecular Weight
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    Da.
    Residues
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    Isoelectric Point
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    Sequence
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      BLAST   FFAS

    Structure Determination
    Method XRAY
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    Chains 2
    Resolution (Å)
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    Rfree
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    Matthews' coefficent 3.57 Rfactor 0.21295
    Waters
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    Solvent Content 65.25

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    Ligand Information
    Ligands
    Metals

    Jmol

     
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    Google Scholar output for 1o4u
    1. The importance of alignment accuracy for molecular replacement
    R Schwarzenbacher, A Godzik - Section D: Biological , 2004 - scripts.iucr.org
     
    2. FRankenstein becomes a cyborg: the automatic recombination and realignment of fold recognition models in CASP6
    J Kosinski, MJ Gajda, IA Cymerman - PROTEINS: , 2005 - Wiley Online Library
     
    3. Microbial biochemistry, physiology, and biotechnology of hyperthermophilic Thermotoga species
    SB Conners, EF Mongodin, MR Johnson - FEMS microbiology , 2006 - Wiley Online Library
     
    4. An iterative knowledge_based scoring function for proteinprotein recognition
    SY Huang, X Zou - Proteins: Structure, Function, and , 2008 - Wiley Online Library
     
    5. Crystal structure of a nicotinate phosphoribosyltransferase from Thermoplasma acidophilum
    DH Shin, N Oganesyan, J Jancarik, H Yokota - Journal of Biological , 2005 - ASBMB
     
    6. The JCSG MR pipeline: optimized alignments, multiple models and parallel searches
    R Schwarzenbacher, A Godzik - Section D: Biological , 2007 - scripts.iucr.org
     
    7. 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
     
    8. Crystal structure of a type II quinolic acid phosphoribosyltransferase (TM1645) from Thermotoga maritima at 2.50 resolution
    R Schwarzenbacher, L Jaroszewski - Proteins: Structure, , 2004 - Wiley Online Library
     
    9. Structural and kinetic characterization of quinolinate phosphoribosyltransferase (hQPRTase) from Homo sapiens
    H Liu, K Woznica, G Catton, A Crawford - Journal of molecular , 2007 - Elsevier
     
    10. Walking through the protein sequence space: Towards new generation of the homology modeling
    ZM Frenkel, EN Trifonov - PROTEINS: Structure, Function, and , 2007 - Wiley Online Library
     
    11. Comprehensive X-ray Structural Studies of the Quinolinate Phosphoribosyl Transferase (BNA6) from Saccharomyces cerevisiae
    E di Luccio, DK Wilson - Biochemistry, 2008 - ACS Publications
     
    12. Subunit interfaces of oligomeric hyperthermophilic enzymes display enhanced compactness
    F Baldasseroni, S Pascarella - International journal of biological , 2009 - Elsevier
     
    13. A novel predicting algorithm of thermostable proteins based on choquet integral with respect to L-measure and hurst exponent
    JI Shieh, YL Liu, KJ Lee, PC Chang - Machine Learning and , 2009 - ieeexplore.ieee.org
     
    14. Carbohydrate utilization pathway analysis in the hyperthermophile Thermotoga maritima
    SB Conners - 2006 - repository.lib.ncsu.edu
     

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    Protein Summary

    The TM1645 gene from Thermotoga maritima encodes the NP_229445 protein, a type II quinolic acid phosphoribosyltransferase (QAPRTase, NadC,

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    , PubMed:15103640), which is an essential enzyme in the NAD+ biosynthetic pathway. This enzyme catalyzes the transfer of a phosphoribosyl moiety from 5-phosphoribosyl-1-pyrophosphate (PRPP) to quinolinic acid (QA), yielding nicotinic acid mononucleotide (NAMN), pyrophosphate and CO2, the last resulting from decarboxylation at position 2 of the quinolinate ring.

    The active enzyme exists as a dimer, where each monomer has two domains with different fold. The N-terminal domain (PF02749) has alpha/beta-Hammerhead fold (SCOP

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    ) and belongs to the family of quinolinic acid phosphoribosyltransferase N-terminal domain (SCOP
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    ). The C-terminal domain (PF01729) has a TIM beta/alpha-barrel fold (SCOP
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    ) and belongs to a superfamily with characteristic incomplete beta/alpha barrel with parallel beta-sheet of 7 strands (Quinolinic acid phosphoribosyltransferase C-terminal domain; SCOP
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    ). DALI top hits are with other pyrophosphorylases like
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    (Z=30),
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    (Z=28),
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    (Z=28),
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    (Z=28).

    Ligand Summary



    References

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