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1o5o

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

    Title Crystal structure of Uracil phosphoribosyltransferase (TM0721) from Thermotoga maritima at 2.30 A resolution. To be published
    Site JCSG
    PDB Id 1o5o Target Id
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    Molecular Characteristics
    Source
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    Alias Ids
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    TPS1227,TM0721, 85035
    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 4
    Resolution (Å)
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    Rfree
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    Matthews' coefficent 2.44 Rfactor 0.16658
    Waters
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    Solvent Content 49.20

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    Ligand Information
    Ligands
    Metals

    Jmol

     
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    Google Scholar output for 1o5o
    1. The importance of alignment accuracy for molecular replacement
    R Schwarzenbacher, A Godzik - Section D: Biological , 2004 - scripts.iucr.org
     
    2. 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
     
    3. Structure of pyrR (Rv1379) from Mycobacterium tuberculosis: a persistence gene and protein drug target
    KA Kantardjieff, C Vasquez, P Castro - Section D: Biological , 2005 - scripts.iucr.org
     
    4. Pyrimidine Salvage Pathway in Mycobacterium tuberculosis
    AD Villela, ZA Sanchez-Quitian - Current Medicinal , 2011 - ingentaconnect.com
     
    5. Three zone segregation of proteins-a comparison of structures
    R Sinha - Potentials, IEEE, 2006 - ieeexplore.ieee.org
     

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    Protein Summary

    The TM0721 gene from Thermotoga maritima encodes an uracil phosphoribosyltransferase (PF00156, COG0035, EC 2.4.2.9). The TM0721 structure adopts a phosphoribosyl-transferase-like fold and shows strong structural similarity with the homolog from another hyperthormophile, Thermus thermophilus (PDB id: 1v9s) with a main-chain rmsd of 1.0 Å over 206 residues and a sequence identity of 57%. Similar results were obtained with homologs from Escherichia coli (PDB id: 2ehj), Aquifex aeolicus (PDB id: 2e55), Burkholderia pseudomallei (PDB id: 3dmp) and Bacillus caldolyticus (PDB id: 1i5e). For more details on the structure and function of this enzyme see Kadziola 2002.

    Ligand Summary



    References

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