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The Open Protein Structure Annotation Network
PDB Keyword
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2ash

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

    Title Crystal structure of Queuine tRNA-ribosyltransferase (EC 2.4.2.29) (tRNA-guanine (tm1561) from THERMOTOGA MARITIMA at 1.90 A resolution. To be published
    Site JCSG
    PDB Id 2ash Target Id
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    Molecular Characteristics
    Source
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    Alias Ids
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    TPS1300,TM1561, 85096
    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 4
    Resolution (Å)
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    Rfree
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    Matthews' coefficent 2.62 Rfactor 0.193
    Waters
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    Solvent Content 52.66

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    Ligand Information
    Ligands
    Metals

    Jmol

     
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    Google Scholar output for 2ash
    1. Crystal structures of tRNA-guanine transglycosylase (TGT) in complex with novel and potent inhibitors unravel pronounced induced-fit adaptations and suggest dimer
    B Stengl, EA Meyer, A Heine, R Brenk - Journal of molecular , 2007 - Elsevier
     
    2. An integrative approach combining noncovalent mass spectrometry, enzyme kinetics and X-ray crystallography to decipher Tgt protein-protein and protein-RNA
    T Ritschel, C Atmanene, K Reuter - Journal of molecular , 2009 - Elsevier
     
    3. Structural and Functional Studies of tRNA-Guanine Transglycosylase: A putative Drug Target for Shigellosis Therapy
    B Stengl - 2006 - archiv.ub.uni-marburg.de
     

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    Protein Summary

    The gene TM1561 from Thermotoga maritima encodes an enzyme queuine tRNA-ribosyltransferase PF01702 COG1549 EC:2.4.2.29.  Some other common names of this enzyme are tRNA-guanine transferase, tRNA guanine transglycosylase, guanine-tRNA transglycosylase, queuine-tRNA transglycosylase, q-insertase.  Queuine is a hypermodified base that occurs in the wobble position of the anticodon of tRNAs of Asp, Asn, His and Tyr .  Queuine tRNA-ribosyltransferase catalyzes the incorporation of queuine into tRNA via a base exchange reaction with guanine.  In eukaryotes, queuine is directly exchanged into tRNA while in eubacteria, a queuine precursor (preQ1) is incorporated and ultimately modified to queuine [Ref].  The enzyme contains a zinc-binding motif.  To date, structures of the enzyme homologues from multiple organisms have been solved (e.g. 1EFZZymomonas mobilis; 1IT8Pyrococcus horikoshii).

    Ligand Summary



    References

    Reviews

    References

     

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