1h3f: Difference between revisions

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{{STRUCTURE_1h3f|  PDB=1h3f  |  SCENE=  }}  
{{STRUCTURE_1h3f|  PDB=1h3f  |  SCENE=  }}  


'''TYROSYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS COMPLEXED WITH TYROSINOL'''
===TYROSYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS COMPLEXED WITH TYROSINOL===




==Overview==
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Bacterial tyrosyl-tRNA synthetases (TyrRS) possess a flexibly linked C-terminal domain of approximately 80 residues, which has hitherto been disordered in crystal structures of the enzyme. We have determined the structure of Thermus thermophilus TyrRS at 2.0 A resolution in a crystal form in which the C-terminal domain is ordered, and confirm that the fold is similar to part of the C-terminal domain of ribosomal protein S4. We have also determined the structure at 2.9 A resolution of the complex of T.thermophilus TyrRS with cognate tRNA(tyr)(G Psi A). In this structure, the C-terminal domain binds between the characteristic long variable arm of the tRNA and the anti-codon stem, thus recognizing the unique shape of the tRNA. The anticodon bases have a novel conformation with A-36 stacked on G-34, and both G-34 and Psi-35 are base-specifically recognized. The tRNA binds across the two subunits of the dimeric enzyme and, remarkably, the mode of recognition of the class I TyrRS for its cognate tRNA resembles that of a class II synthetase in being from the major groove side of the acceptor stem.
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{{ABSTRACT_PUBMED_12110594}}


==About this Structure==
==About this Structure==
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[[Category: Yaremchuk, A.]]
[[Category: Yaremchuk, A.]]
[[Category: Aminoacyl-trna synthetase]]
[[Category: Aminoacyl-trna synthetase]]
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Revision as of 06:33, 1 July 2008

File:1h3f.png

Template:STRUCTURE 1h3f

TYROSYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS COMPLEXED WITH TYROSINOLTYROSYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS COMPLEXED WITH TYROSINOL

Template:ABSTRACT PUBMED 12110594

About this StructureAbout this Structure

1H3F is a Single protein structure of sequence from Thermus thermophilus. Full crystallographic information is available from OCA.

ReferenceReference

Class I tyrosyl-tRNA synthetase has a class II mode of cognate tRNA recognition., Yaremchuk A, Kriklivyi I, Tukalo M, Cusack S, EMBO J. 2002 Jul 15;21(14):3829-40. PMID:12110594

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