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    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 282046
    Molecular Characteristics
    Source Thermotoga maritima msb8
    Alias Ids TPS1188,TM0166, 3.40.1190.10, 83902 Molecular Weight 48865.97 Da.
    Residues 430 Isoelectric Point 6.55
    Sequence maylevlrylyhkrpmgkvkpglerismllsklgnphleyktihiggtngkgsvanmvsnilvsqgyrv gsyysphlstfrerirlneeyiseedvvkiyetmepilneldkeeifspsffevvtamaflyfaeknvd iavlevglggrldatnvvfplcstivtvdrdhektlgytieqiaweksgiikervplvtgerkrealkv medvarkkssrmyvidkdfsvkvkslklhenrfdycgentfedlvltmngphqienagvalktleatgl plsekaireglknaknlgrfeilekngkmyildgahnphgaeslvrslklyfngeplslvigilddknr edilrkytgifervivtrvpsprmkdmnslvdmakkffknveviedpleaiesteratvvtgslflvgy vreflttgkineewkl
      BLAST   FFAS

    Structure Determination
    Method XRAY Chains 1
    Resolution (Å) 2.10 Rfree 0.24421
    Matthews' coefficent 2.80 Rfactor 0.18107
    Waters 323 Solvent Content 55.67

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    Ligand Information


    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

    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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