1h3f: Difference between revisions

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[[Image:1h3f.gif|left|200px]]
[[Image:1h3f.gif|left|200px]]


{{Structure
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The line below this paragraph, containing "STRUCTURE_1h3f", creates the "Structure Box" on the page.
|SITE= <scene name='pdbsite=AC1:Tyb+Binding+Site+For+Chain+B'>AC1</scene>
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{{STRUCTURE_1h3f| PDB=1h3f  | SCENE= }}  
|RELATEDENTRY=
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1h3f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h3f OCA], [http://www.ebi.ac.uk/pdbsum/1h3f PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1h3f RCSB]</span>
}}


'''TYROSYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS COMPLEXED WITH TYROSINOL'''
'''TYROSYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS COMPLEXED WITH TYROSINOL'''
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[[Category: Tukalo, M.]]
[[Category: Tukalo, M.]]
[[Category: Yaremchuk, A.]]
[[Category: Yaremchuk, A.]]
[[Category: aminoacyl-trna synthetase]]
[[Category: Aminoacyl-trna synthetase]]
[[Category: atp + l-tyrosine + trna(tyr)->amp + ppi + l-tyrosyl-trna(ty class i aminoacyl-trna synthetase]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 18:23:07 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:56:53 2008''

Revision as of 18:23, 2 May 2008

File:1h3f.gif

Template:STRUCTURE 1h3f

TYROSYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS COMPLEXED WITH TYROSINOL


OverviewOverview

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 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 Page seeded by OCA on Fri May 2 18:23:07 2008

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