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2o5r

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

    Title Crystal structure of Glutamyl-tRNA synthetase 1 (EC 6.1.1.17) (Glutamate-tRNA ligase 1) (GluRS 1) (TM1351) from Thermotoga maritima at 2.5 A resolution. To be published
    Site JCSG
    PDB Id 2o5r Target Id 283212
    Molecular Characteristics
    Source Thermotoga maritima msb8
    Alias Ids TPS1279,TM1351, 84718 Molecular Weight 54604.11 Da.
    Residues 469 Isoelectric Point 5.64
    Sequence mvrvrfapsptgflhvggartalfnflfarkekgkfilriedtdlersereyeeklmeslrwlgllwde gpdvggdhgpyrqserveiyrehaerlvkegkayyvyaypeeieemrekllsegkaphysqemfekfdt perrreyeekglrpavffkmprkdyvlndvvkgevvfktgaigdfvimrsnglptynfacvvddmlmei thvirgddhlsntlrqlalyeafekappvfahvstilgpdgkklskrhgatsveafrdmgylpealvny lallgwshpegkelltleelissfsldrlspnpaifdpqklkwmngyylrnmpieklaelakpffekag ikiideeyfkkvleitkervevlsefpeesrfffedpapveipeemkevfsqlkeelqnvrwtmeeitp vfkkvlkqhgvkpkefymtlrrvltgreegpelvniipllgkeiflrrierslgg
      BLAST   FFAS

    Structure Determination
    Method XRAY Chains 1
    Resolution (Å) 2.34 Rfree 0.268
    Matthews' coefficent 3.53 Rfactor 0.234
    Waters 60 Solvent Content 65.11

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    Ligand Information
    Ligands
    Metals

    Jmol

     
    Google Scholar output for 2o5r
    1. Structure of nondiscriminating glutamyl-tRNA synthetase from Thermotoga maritima
    T Ito, N Kiyasu, R Matsunaga, S Takahashi - Section D: Biological , 2010 - scripts.iucr.org
     
    2. Structural and functional consequences of mutating a proteobacteria-specific surface residue in the catalytic domain of E. coli GluRS
    S Dasgupta, D Manna, G Basu - FEBS letters, 2012 - Elsevier
     
    3. A structural approach of R A-protein recognition and kinetics of binding in two examples: tR A aminoacylation by arginyl-tR A synthetase and 7SK stabilization
    E Uchikawa - 2011 - scd-theses.u-strasbg.fr
     

    Protein Summary

    The TM1351 (also known as gltX) gene (PF00749, cd00808, cl00015) from Thermotoga maritima encodes for a Glutamyl-tRNA synthetase (EC:6.1.1.17). There is clear sequence and structure similarity to glutamyl- and glutaminyl-tRNA synthetases (COG0008). The structure adopts a Rossman fold and has several additional small domains according to CATH (2o5r-CATH), including two of which are orthogonal bundles and additional two are related to the synthetase activity. Another PSI determined structures with a similar core fold is 3fnr.

    Notics that it has sequence similarity to tRNA synthetases class I (PF00749 / PF01921) and glutamyl- and glutaminyl-tRNA synthetases.

    Ligand Summary



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