1h3f

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==Overview==
==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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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.
==About this Structure==
==About this Structure==
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[[Category: atp + l-tyrosine + trna(tyr)->amp + ppi + l-tyrosyl-trna(ty class i aminoacyl-trna synthetase]]
[[Category: atp + l-tyrosine + trna(tyr)->amp + ppi + l-tyrosyl-trna(ty class i aminoacyl-trna synthetase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:45:50 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:56:59 2008''

Revision as of 10:57, 21 February 2008


1h3f, resolution 2.00Å

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TYROSYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS COMPLEXED WITH TYROSINOL

Overview

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.

About this Structure

1H3F is a Single protein structure of sequence from Thermus thermophilus with and as ligands. Known structural/functional Site: . Full crystallographic information is available from OCA.

Reference

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[[Category: atp + l-tyrosine + trna(tyr)->amp + ppi + l-tyrosyl-trna(ty class i aminoacyl-trna synthetase]]

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