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1JH3

Solution structure of tyrosyl-tRNA synthetase C-terminal domain.

Summary for 1JH3
Entry DOI10.2210/pdb1jh3/pdb
Related2TS1
NMR InformationBMRB: 5070
DescriptorTYROSYL-TRNA SYNTHETASE (1 entity in total)
Functional Keywordsaminoacyl-trna synthetase, anticodon-arm binding domain, ligase
Biological sourceGeobacillus stearothermophilus
Cellular locationCytoplasm: P00952
Total number of polymer chains1
Total formula weight12001.54
Authors
Guijarro, J.I.,Pintar, A.,Prochnicka-Chalufour, A.,Guez, V.,Gilquin, B.,Bedouelle, H.,Delepierre, M. (deposition date: 2001-06-27, release date: 2002-03-20, Last modification date: 2024-05-29)
Primary citationGuijarro, J.I.,Pintar, A.,Prochnicka-Chalufour, A.,Guez, V.,Gilquin, B.,Bedouelle, H.,Delepierre, M.
Structure and Dynamics of the Anticodon Arm Binding Domain of Bacillus stearothermophilus Tyrosyl-tRNA Synthetase
Structure, 10:311-317, 2002
Cited by
PubMed Abstract: The structure of a recombinant protein, TyrRS(delta4), corresponding to the anticodon arm binding domain of Bacillus stearothermophilus tyrosyl-tRNA synthetase, has been solved, and its dynamics have been studied by nuclear magnetic resonance (NMR). It is the first structure described for such a domain of a tyrosyl-tRNA synthetase. It consists of a five-stranded beta sheet, packed against two alpha helices on one side and one alpha helix on the other side. A large part of the domain is structurally similar to other functionally unrelated RNA binding proteins. The basic residues known to be essential for tRNA binding and charging are exposed to the solvent on the same face of the molecule. The structure of TyrRS(delta4), together with previous mutagenesis data, allows one to delineate the region of interaction with tRNATyr.
PubMed: 12005430
DOI: 10.1016/S0969-2126(02)00699-8
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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