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2gi3

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

    Title Crystal structure of Glutamyl-tRNA(Gln) amidotransferase subunit A (tm1272) from THERMOTOGA MARITIMA at 1.80 A resolution. To be published
    Site JCSG
    PDB Id 2gi3 Target Id
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    Molecular Characteristics
    Source
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    Alias Ids
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    TPS1274,TM1272
    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 1
    Resolution (Å)
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    Rfree
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    Matthews' coefficent 2.83 Rfactor 0.175
    Waters
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    Solvent Content 56.20

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    Ligand Information
    Ligands
    Metals

    Jmol

     
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    Google Scholar output for 2gi3
    1. On the combination of molecular replacement and single-wavelength anomalous diffraction phasing for automated structure determination
    S Panjikar, V Parthasarathy, VS Lamzin - Section D: Biological , 2009 - scripts.iucr.org
     
    2. Insights into tRNA-dependent amidotransferase evolution and catalysis from the structure of the Aquifex aeolicus enzyme
    J Wu, W Bu, K Sheppard, M Kitabatake - Journal of molecular , 2009 - Elsevier
     
    3. Structure and characterization of amidase from Rhodococcus sp. N-771: Insight into the molecular mechanism of substrate recognition
    A Ohtaki, K Murata, Y Sato, K Noguchi - et Biophysica Acta (BBA , 2010 - Elsevier
     
    4. Structural Relationship between the Active Sites of _-Lactam-Recognizing and Amidase Signature Enzymes: Convergent Evolution?
    RF Pratt, MJ McLeish - Biochemistry, 2010 - ACS Publications
     

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    Protein Summary

    The gene TM1272 from Thermotoga maritima encodes glutamyl- and/or aspartyl-tRNA  amidotransferase (AdTase) subunit A  [Ref] E.C.6.3.5.6, a member of  amidases family PF01425 COG0154.  The enzyme is heterodimeric/possesses two clearly defined structural domains. They are widespread, being found in both prokaryotes and eukaryotes.  These enzymes posses a unique, highly conserved Ser-Ser-Lys catalytic triad used for amide hydrolysis, although the catalytic mechanism for acyl-enzyme intermediate formation can differ between enzymes [Ref].  Two different types of AdTase are currently known. One is a heterotrimeric enzyme, a typical form in Gram-positive eubacteria. In contrast, AdTase from archaebacteria consists of two different subunits/domains [Ref], as in the given case.

    Ligand Summary



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