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2hxv

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

    Title Crystal structure of Diaminohydroxyphosphoribosylaminopyrimidine deaminase/ 5-amino-6-(5-phosphoribosylamino)uracil reductase (TM1828) from Thermotoga maritima at 1.80 A resolution. To be published
    Site JCSG
    PDB Id 2hxv Target Id 283681
    Molecular Characteristics
    Source Thermotoga maritima msb8
    Alias Ids TPS1318,TM1828, _0078.007649_, 289577 Molecular Weight 38863.68 Da.
    Residues 348 Isoelectric Point 6.78
    Sequence myetfmkraielakkglgrvnpnppvgavvvkdgriiaegfhpyfggphaermaiesarkkgedlrgat livtlepcdhhgktppctdliiesgiktvvigtrdpnpvsgngvekfrnhgieviegvleeevkklcef fityvtkkrpfvalkyastldgkiadhrgdskwitdklrfkvhemrniysavlvgagtvlkdnpqltcr lkegrnpvrvildrkgvlsgkvfrvfeenarvivfteseeaeypphvekalsdcsvesilrnlyerdid svlveggskvfsefldhadvvfgfystkifgkgldvfsgylsdvsvppkfkvvnvefsdseflvemrpcsre
      BLAST   FFAS

    Structure Determination
    Method XRAY Chains 1
    Resolution (Å) 1.80 Rfree 0.195
    Matthews' coefficent 2.34 Rfactor 0.16
    Waters 205 Solvent Content 47.06

    Pathway

    Reactions found in Metabolic Reconstruction for TM1828

    Name: diaminohydroxyphosphoribosylaminopyrimidine deaminase
    Metabolic Subsystem: Riboflavin Metabolism
    Reaction: : 25dhpp + h + h2o --> 5apru + nh4
    Classification: EC:3.5.4.26
     
    Name: 5-amino-6-(5-phosphoribosylamino)uracil reductase
    Metabolic Subsystem: Riboflavin Metabolism
    Reaction: : 5apru + h + nadph --> 5aprbu + nadp
    Classification: EC:1.1.1.193
     

    Ligand Information
    Ligands
    Metals

    Jmol

     
    Google Scholar output for 2hxv
    1. Decision-making in structure solution using Bayesian estimates of map quality: the PHENIX AutoSol wizard
    TC Terwilliger, PD Adams, RJ Read - Section D: Biological , 2009 - scripts.iucr.org
     
    2. Complex Structure of Bacillus subtilis RibG
    SC Chen, YH Lin, HC Yu, SH Liaw - Journal of Biological Chemistry, 2009 - ASBMB
     

    Protein Summary

    The TM1828 from T. maritima - is a bifunctional protein found in bacteria and archaea. Its N-terminal part contains riboflavin-specific deaminase (cd01284), while  C-terminal part contains pyrimidine reductase (COG1985, ribD).

    TM1828 functions are interdependent with the folowing genomic neighbors having similar phylogenetic cooccurrence: TM1827 [Q9X2E7] - riboflavin synthase, alpha subunit; RIBH [RISB_THEMA] - 6,7-dimethyl-8-ribityllumazine synthase (EC 2.5.1.9); RIBA [GCH2_THEMA] - riboflavin biosynthesis protein ribA.

    TM1828 has strong structural similarity to: PDB:2b3z (DALI Z-score 38.8; RMSD 2.2; 40% identity within 337 superimposed residues), PDB:1d1g (DALI Z-score 17.0; RMSD 2.4; 22% identity within 156 superimposed residues), PDB:1uaq (DALI Z-score 15.5; RMSD 2.5; 29% identity within 126 superimposed residues), PDB:2g84 (DALI Z-score 15.2; RMSD 2.6; 29% identity within 119 superimposed residues), PDB:1teo (DALI Z-score 15.0; RMSD 1.9 ; 35% identity within 116 superimposed residues).

    Analysis of the crystallographic packing of TM1828 using the PQS server {Henrick, 1998 #73} indicates that a dimer is the biologically relevant form.

    Ligand Summary



    References

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