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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
1999-5-20
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pubmed:databankReference |
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pubmed:abstractText |
E. coli threonyl-tRNA synthetase (ThrRS) is a class II enzyme that represses the translation of its own mRNA. We report the crystal structure at 2.9 A resolution of the complex between tRNA(Thr) and ThrRS, whose structural features reveal novel strategies for providing specificity in tRNA selection. These include an amino-terminal domain containing a novel protein fold that makes minor groove contacts with the tRNA acceptor stem. The enzyme induces a large deformation of the anticodon loop, resulting in an interaction between two adjacent anticodon bases, which accounts for their prominent role in tRNA identity and translational regulation. A zinc ion found in the active site is implicated in amino acid recognition/discrimination.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0092-8674
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
30
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pubmed:volume |
97
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
371-81
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:10319817-Amino Acyl-tRNA Synthetases,
pubmed-meshheading:10319817-Bacterial Proteins,
pubmed-meshheading:10319817-Base Sequence,
pubmed-meshheading:10319817-Binding Sites,
pubmed-meshheading:10319817-Catalytic Domain,
pubmed-meshheading:10319817-Dimerization,
pubmed-meshheading:10319817-Enzyme Activation,
pubmed-meshheading:10319817-Escherichia coli,
pubmed-meshheading:10319817-Genetic Complementation Test,
pubmed-meshheading:10319817-Molecular Mimicry,
pubmed-meshheading:10319817-Molecular Sequence Data,
pubmed-meshheading:10319817-Nucleic Acid Conformation,
pubmed-meshheading:10319817-Protein Structure, Secondary,
pubmed-meshheading:10319817-Protein Structure, Tertiary,
pubmed-meshheading:10319817-RNA, Messenger,
pubmed-meshheading:10319817-RNA, Transfer, Amino Acyl,
pubmed-meshheading:10319817-Sequence Homology, Amino Acid,
pubmed-meshheading:10319817-Zinc
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pubmed:year |
1999
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pubmed:articleTitle |
The structure of threonyl-tRNA synthetase-tRNA(Thr) complex enlightens its repressor activity and reveals an essential zinc ion in the active site.
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pubmed:affiliation |
UPR 9004 Biologie Structurale, Institut de Génétique et de Biologie Moléculaire et Cellulaire, CNRS/INSERM/ULP, Illkirch, France.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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