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1o4v

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

    Title Crystal structure of a phosphoribosylaminoimidazole mutase PurE (TM0446) from Thermotoga maritima at 1.77 A resolution. Proteins 55 474-478 2004
    Site JCSG
    PDB Id 1o4v Target Id 282319
    Molecular Characteristics
    Source Thermotoga maritima msb8
    Alias Ids TPS1205,TM0446, 282164 Molecular Weight 18616.67 Da.
    Residues 171 Isoelectric Point 6.33
    Sequence mprvgiimgsdsdlpvmkqaaeileefgidyeitivsahrtpdrmfeyaknaeergieviiagaggaah lpgmvasithlpvigvpvktstlngldslfsivqmpggvpvatvainnaknagilaasilgikypeiar kvkeykermkrevlekaqrleqigykeylnqke
      BLAST   FFAS

    Structure Determination
    Method XRAY Chains 1
    Resolution (Å) 1.77 Rfree 0.18177
    Matthews' coefficent 2.18 Rfactor 0.14981
    Waters 118 Solvent Content 43.12

    Pathway

    Reactions found in Metabolic Reconstruction for TM0446

    Name: phosphoribosylaminoimidazole carboxylase
    Other genes that carryout this rxn: TM0447
    Metabolic Subsystem: Purine Biosynthesis
    Reaction: : air + co2 <==> 5aizc + h
    Classification: EC:4.1.1.21
     

    Ligand Information
    Ligands
    Metals

    Jmol

     
    Google Scholar output for 1o4v
    1. The importance of alignment accuracy for molecular replacement
    R Schwarzenbacher, A Godzik - Section D: Biological , 2004 - scripts.iucr.org
     
    2. SPINE workshop on automated X-ray analysis: a progress report
    M Bahar, C Ballard, SX Cohen, KD Cowtan - Section D: Biological , 2006 - scripts.iucr.org
     
    3. 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
     
    4. Crystal structure of a phosphoribosylaminoimidazole mutase PurE (TM0446) from Thermotoga maritima at 1.77_ resolution
    R Schwarzenbacher, L Jaroszewski - Proteins: Structure, , 2004 - Wiley Online Library
     
    5. Crystal structure of PurE (BA0288) from Bacillus anthracis at 1.8 resolution
    MP Boyle, AK Kalliomaa, V Levdikov - PROTEINS: , 2005 - Wiley Online Library
     
    6. Improvement of molecular-replacement models with Sculptor
    G Bunkoczi, RJ Read - Acta Crystallographica Section D: Biological , 2011 - scripts.iucr.org
     
    7. Treponema denticola PurE Is a Bacterial AIR Carboxylase
    S Tranchimand, CM Starks, II Mathews - Biochemistry, 2011 - ACS Publications
     
    8. Prdiction des rsidus impliqus dans le noyau du repliement et classification structurale de fragments protiques en interaction.
    N Prudhomme - 2009 - hal.archives-ouvertes.fr
     

    Protein Summary

    The TM0446 gene of Thermotoga maritima encodes the NP_228256 protein, a N5-Carboxyaminoimidazole ribonucleotide (N5-CAIR) mutase (PurE, AIRC, EC 4.1.1.21, member of COG0041, PF00731), that catalyzes the only C-C-bond-forming reaction in de novo purine biosynthesis, the formation of 4-carboxy-5-aminoimidazole ribonucleotide (CAIR) (PubMed:15048837).

    1o4v has a flavodoxin-like fold (SCOP sunid:52171) with 3 layers, a/b/a; parallel beta-sheet of 5 strand, order 21345 and belongs to family of N5-CAIR mutases (SCOP sunid:52256). Dali top hits are with the carboxylases/mutases 1xmp (Z-scr=28), 2fwa (Z-scr=27),

    PurE proteins are highly conserved and designated as Class I or Class II according to their enzymatic activity. Class I enzymes, found in yeast, plants, and prokaryotes, catalyze the second of a two-step conversion of 5-aminoimidazole ribonucleotide (AIR), via the intermediate N5-carboxyaminoimidazole ribonucleotide (N5-CAIR), to 4-carboxy-5-aminoimidazole ribonucleotide (CAIR) (PubMed:8117684, 10074353). The conversion of AIR to N5-CAIR is catalyzed by N5-CAIR synthetase (PurK) in the presence of ATP and bicarbonate. Class II enzymes from higher eukaryotes catalyze the conversion of AIR to CAIR directly, in the presence of bicarbonate or CO2. Therefore, Class I PurE proteins function as phosphoribosylaminoimidazole mutases, while Class II enzymes are carboxylases.

    Ligand Summary



    References

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