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PDBsum entry 2dr2
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References listed in PDB file
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Key reference
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Title
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Structure of human tryptophanyl-Trna synthetase in complex with trnatrp reveals the molecular basis of trna recognition and specificity.
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Authors
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N.Shen,
L.Guo,
B.Yang,
Y.Jin,
J.Ding.
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Ref.
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Nucleic Acids Res, 2006,
34,
3246-3258.
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PubMed id
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Abstract
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Aminoacyl-tRNA synthetases (aaRSs) are a family of enzymes responsible for the
covalent link of amino acids to their cognate tRNAs. The selectivity and
species-specificity in the recognitions of both amino acid and tRNA by aaRSs
play a vital role in maintaining the fidelity of protein synthesis. We report
here the first crystal structure of human tryptophanyl-tRNA synthetase (hTrpRS)
in complex with tRNA(Trp) and Trp which, together with biochemical data, reveals
the molecular basis of a novel tRNA binding and recognition mechanism. hTrpRS
recognizes the tRNA acceptor arm from the major groove; however, the 3' end CCA
of the tRNA makes a sharp turn to bind at the active site with a deformed
conformation. The discriminator base A73 is specifically recognized by an
alpha-helix of the unique N-terminal domain and the anticodon loop by an
alpha-helix insertion of the C-terminal domain. The N-terminal domain appears to
be involved in Trp activation, but not essential for tRNA binding and acylation.
Structural and sequence comparisons suggest that this novel tRNA binding and
recognition mechanism is very likely shared by other archaeal and eukaryotic
TrpRSs, but not by bacterial TrpRSs. Our findings provide insights into the
molecular basis of tRNA specificity and species-specificity.
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