1h3e

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[[Image:1h3e.gif|left|200px]]<br /><applet load="1h3e" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1h3e.gif|left|200px]]
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caption="1h3e, resolution 2.90&Aring;" />
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'''TYROSYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS COMPLEXED WITH WILD-TYPE TRNATYR(GUA) AND WITH ATP AND TYROSINOL'''<br />
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{{Structure
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|PDB= 1h3e |SIZE=350|CAPTION= <scene name='initialview01'>1h3e</scene>, resolution 2.90&Aring;
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|SITE= <scene name='pdbsite=AC1:Tyb+Binding+Site+For+Chain+A'>AC1</scene>
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|LIGAND= <scene name='pdbligand=ATP:ADENOSINE-5'-TRIPHOSPHATE'>ATP</scene> and <scene name='pdbligand=TYB:TYROSINAL'>TYB</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Tyrosine--tRNA_ligase Tyrosine--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.1 6.1.1.1]
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|GENE=
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}}
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'''TYROSYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS COMPLEXED WITH WILD-TYPE TRNATYR(GUA) AND WITH ATP AND TYROSINOL'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1H3E is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus] with <scene name='pdbligand=ATP:'>ATP</scene> and <scene name='pdbligand=TYB:'>TYB</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Tyrosine--tRNA_ligase Tyrosine--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.1 6.1.1.1] Known structural/functional Site: <scene name='pdbsite=AC1:Tyb+Binding+Site+For+Chain+A'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H3E OCA].
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1H3E is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H3E OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12110594 12110594]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/12110594 12110594]
[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Thermus thermophilus]]
[[Category: Thermus thermophilus]]
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[[Category: class i aminoacyl-trna synthetase: atp + l-tyrosine + trna(tyr) -> amp + ppi + l-tyrosyl-trna(tyr)]]
[[Category: class i aminoacyl-trna synthetase: atp + l-tyrosine + trna(tyr) -> amp + ppi + l-tyrosyl-trna(tyr)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:56:58 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:31:37 2008''

Revision as of 09:31, 20 March 2008


PDB ID 1h3e

Drag the structure with the mouse to rotate
, resolution 2.90Å
Sites:
Ligands: and
Activity: Tyrosine--tRNA ligase, with EC number 6.1.1.1
Coordinates: save as pdb, mmCIF, xml



TYROSYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS COMPLEXED WITH WILD-TYPE TRNATYR(GUA) AND WITH ATP AND 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

1H3E is a Protein complex structure of sequences from Thermus thermophilus. 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: class i aminoacyl-trna synthetase: atp + l-tyrosine + trna(tyr) -> amp + ppi + l-tyrosyl-trna(tyr)]]

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