Source:http://linkedlifedata.com/resource/pubmed/id/20606262
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
Pt 7
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pubmed:dateCreated |
2010-7-7
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pubmed:abstractText |
Aminoacyl-tRNA synthetases produce aminoacyl-tRNAs from the substrate tRNA and its cognate amino acid with the aid of ATP. Two types of glutamyl-tRNA synthetase (GluRS) have been discovered: discriminating GluRS (D-GluRS) and nondiscriminating GluRS (ND-GluRS). D-GluRS glutamylates tRNA(Glu) only, while ND-GluRS glutamylates both tRNA(Glu) and tRNA(Gln). ND-GluRS produces the intermediate Glu-tRNA(Gln), which is converted to Gln-tRNA(Gln) by Glu-tRNA(Gln) amidotransferase. Two GluRS homologues from Thermotoga maritima, TM1875 and TM1351, have been biochemically characterized and it has been clarified that only TM1875 functions as an ND-GluRS. Furthermore, the crystal structure of the T. maritima ND-GluRS, TM1875, was determined in complex with a Glu-AMP analogue at 2.0 A resolution. The T. maritima ND-GluRS contains a characteristic structure in the connective-peptide domain, which is inserted into the catalytic Rossmann-fold domain. The glutamylation ability of tRNA(Gln) by ND-GluRS was measured in the presence of the bacterial Glu-tRNA(Gln) amidotransferase GatCAB. Interestingly, the glutamylation efficiency was not affected even in the presence of excess GatCAB. Therefore, GluRS avoids competition with GatCAB and glutamylates tRNA(Gln).
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
1399-0047
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pubmed:author | |
pubmed:issnType |
Electronic
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pubmed:volume |
66
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
813-20
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pubmed:meshHeading |
pubmed-meshheading:20606262-Amino Acid Sequence,
pubmed-meshheading:20606262-Conserved Sequence,
pubmed-meshheading:20606262-Crystallography, X-Ray,
pubmed-meshheading:20606262-Glutamate-tRNA Ligase,
pubmed-meshheading:20606262-Models, Molecular,
pubmed-meshheading:20606262-Molecular Sequence Data,
pubmed-meshheading:20606262-Protein Structure, Tertiary,
pubmed-meshheading:20606262-RNA, Transfer, Amino Acyl,
pubmed-meshheading:20606262-Sequence Alignment,
pubmed-meshheading:20606262-Structural Homology, Protein,
pubmed-meshheading:20606262-Thermotoga maritima
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pubmed:year |
2010
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pubmed:articleTitle |
Structure of nondiscriminating glutamyl-tRNA synthetase from Thermotoga maritima.
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pubmed:affiliation |
Department of Biophysics and Biochemistry, Graduate School of Science, The University of Tokyo, Bunkyo-ku, Tokyo, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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