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1o5z

    Table of contents
    1. 1. Protein Summary

    Title Crystal structure of Folylpolyglutamate synthase (TM0166) from Thermotoga maritima at 2.10 A resolution. To be published
    Site JCSG
    PDB Id 1o5z Target Id
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    Molecular Characteristics
    Source
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    Alias Ids
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    TPS1188,TM0166, 3.40.1190.10, 83902
    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 1
    Resolution (Å)
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    Rfree
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    Matthews' coefficent 2.80 Rfactor 0.18107
    Waters
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    Solvent Content 55.67

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    Ligand Information
    Ligands
    Metals

    Jmol

     
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    Google Scholar output for 1o5z
    1. The importance of alignment accuracy for molecular replacement
    R Schwarzenbacher, A Godzik - Section D: Biological , 2004 - scripts.iucr.org
     
    2. Structure, Function and Dynamics in the mur Family of Bacterial Cell Wall Ligases
    CA Smith - Journal of molecular biology, 2006 - Elsevier
     
    3. The JCSG MR pipeline: optimized alignments, multiple models and parallel searches
    R Schwarzenbacher, A Godzik - Section D: Biological , 2007 - scripts.iucr.org
     
    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. A fold-recognition approach to loop modeling
    C Levefelt, D Lundh - Journal of molecular modeling, 2006 - Springer
     
    6. Structures of Mycobacterium tuberculosis folylpolyglutamate synthase complexed with ADP and AMPPCP
    PG Young, CA Smith, P Metcalf - Section D: Biological , 2008 - scripts.iucr.org
     
    7. Mutation of Gly51 to serine in the P-loop of Lactobacillus casei folylpolyglutamate synthetase abolishes activity by altering the conformation of two adjacent loops
    CA Smith, JA Cross, AL Bognar, X Sun - Crystallographica Section D , 2006 - scripts.iucr.org
     
    8. Purification, crystallization and preliminary X-ray analysis of Mycobacterium tuberculosis folylpolyglutamate synthase (MtbFPGS)
    PG Young, CA Smith, X Sun, EN Baker - Section F: Structural , 2006 - scripts.iucr.org
     

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    Protein Summary

    The TM0166 gene from Thermotoga maritima encodes a folylpolyglutamate synthase (FPGS) (PF02825, COG0285), an ATP-dependent enzyme that catalyzes the addition of a polyglutamate tail to folate and folate derivatives thereby playing a key role in the retention of intracellular folate. FPGS has been employed in the production of anticancer drugs with increased cytotoxicity [Ref] and is also considered an attractive target for anti-microbial therapy [Ref]. change.[Ref]

    The structure reveals a two-domain organization and is highly similar (main-chain rmsd 1.7 Å over 358 residues with a sequence identity of 33%) with the FPGS from Lactobacillus casei (PDB id: 2fgs [Ref]). The active site of TM0116, located in a large interdomain cleft adjacent to an ATP-binding P-loop motif (GTNGKGS, TM0116 residues 46-51), contains an unidentified ligand that by comparison with 2fgs and 1w7k is likely to be a mimetic for ATP. A second unidentified ligand, located along a C-terminal cleft, is likely to indicate the site of folate binding. See [Ref] for more details on the structure and active site.

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