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 Imidazole glycerol phosphate synthase subunit hisF (EC 4.1.3.-) (tm1036) from Thermotoga maritima at 1.64 A resolution. To be published
    Site JCSG
    PDB Id 2a0n Target Id 282903
    Molecular Characteristics
    Source Thermotoga maritima msb8
    Alias Ids TPS1255,TM1036, 89960 Molecular Weight 27717.37 Da.
    Residues 253 Isoelectric Point 5.19
    Sequence mlakriiacldvkdgrvvkgtnfenlrdsgdpvelgkfyseigidelvflditasvekrktmlelvekv aeqidipftvgggihdfetaselilrgadkvsintaavenpslitqiaqtfgsqavvvaidakrvdgef mvftysgkkntgillrdwvvevekrgageilltsidrdgtksgydtemirfvrplttlpiiasggagkm ehfleaflagadaalaasvfhfreidvrelkeylkkhgvnvrlegl
      BLAST   FFAS

    Structure Determination
    Method XRAY Chains 1
    Resolution (Å) 1.64 Rfree 0.192
    Matthews' coefficent 3.29 Rfactor 0.167
    Waters 281 Solvent Content 62.33

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    Ligand Information


    Google Scholar output for 2a0n
    1. Exploring Symmetry as an Avenue to the Computational Design of Large Protein Domains
    C Fortenberry, EA Bowman, W Proffitt - Journal of the , 2011 - ACS Publications
    2. Energy transfer in nonlinear network models of proteins
    F Piazza, YH Sanejouand - EPL (Europhysics Letters), 2009 - iopscience.iop.org
    3. Protein structural classification and family identification by multifractal analysis and wavelet spectrum
    SM Zhu, ZG Yu, A Vo - Chinese Physics B, 2011 - iopscience.iop.org

    Protein Summary

    The TN1036 gene from Thermotoga maritima encodes the cyclase subunit of  imidazole-glycerol-3-phosphate synthase HisF (HisF-cyclase).  This family belong to the common phosphate binding site TIM barrel family PF00977.  Imidazole glycerol phosphate synthase catalyzes the fifth step of histidine biosynthesis, the formation of the imidazole ring.  The enzyme converts N1-(5'-phosphoribulosyl)-formimino-5-aminoimidazole-4-carboxamide ribonucleotide (PRFAR) to imidazole glycerol phosphate (ImGP) and 5'-(5-aminoimidazole-4-carboxamide) ribonucleotide (AICAR). This conversion involves two tightly coupled reactions in distinct active sites of HisF. The two catalytic domains can be fused, like in fungi and plants, or preformed within  a heterodimer (HisH-glutaminase and HisF-cyclase), like in bacteria.

    Ligand Summary





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