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1zcz

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

    Title Crystal structure of AICAR transformylase IMP cyclohydrolase (TM1249) from Thermotoga maritima at 1.88 A resolution. Proteins 71 1042-1049 2008
    Site JCSG
    PDB Id 1zcz Target Id
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    Molecular Characteristics
    Source
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    Alias Ids
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    TPS1443,TM1249
    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 2.30 Rfactor 0.156
    Waters
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    Solvent Content 46.12

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    Ligand Information
    Ligands
    Metals

    Jmol

     
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    Google Scholar output for 1zcz
    1. Autoindexing with outlier rejection and identification of superimposed lattices
    NK Sauter, BK Poon - Journal of Applied Crystallography, 2010 - scripts.iucr.org
     
    2. Crystal structure of AICAR transformylase IMP cyclohydrolase (TM1249) from Thermotoga maritima at 1.88 resolution
    HL Axelrod, D McMullan, S Krishna - Proteins: Structure, , 2008 - Wiley Online Library
     

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    Protein Summary

    Phosphoribosyl-aminoimidazole-carboxamide formyltransferase / IMP Cyclohydrolase (TM1249; ATIC; purH) from Thermotoga maritima is a bifunctional enzyme with folate-dependent AICAR transformylase and IMP cyclohydrolase activities that catalyzes the last two steps of purine biosynthesis.

    TM1249 has two functional domains. The N-terminal Inosine monophosphate cyclohydrolase domain (cd01421; EC:3.5.4.10) similar to MGS-like domain (pfam02142) converts the formyl-5-aminoimidazole-4-carboxamide-ribonucleotide to inosine monophosphate. The C-terminal ATIC formylase domain (pfam01808; EC:2.1.2.3) formylates 5-aminoimidazole-4-carboxamide-ribonucleotide. Those two final steps in de novo purine production is catalysed first by C-terminal domain and then by N-terminal domain.

    TM1249 and similar purH (PDB:1p4r) have two structural domains, first with methylglyoxal synthase-like fold (SCOP sunid:52334) 3 layers, ?/?/?; parallel beta-sheet of 5 strands, order 32145, and second domain with cytidine deaminase-like fold (SCOP sunid:53926) core: ?-?(2)-(?-?)2; 3 layers (?/?/?); mixed ?-sheet of 4 strands, order 2134; strand 2 is antiparallel to the rest.


    Ligand Summary



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