1h3e
From Proteopedia
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|PDB= 1h3e |SIZE=350|CAPTION= <scene name='initialview01'>1h3e</scene>, resolution 2.90Å | |PDB= 1h3e |SIZE=350|CAPTION= <scene name='initialview01'>1h3e</scene>, resolution 2.90Å | ||
|SITE= <scene name='pdbsite=AC1:Tyb+Binding+Site+For+Chain+A'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Tyb+Binding+Site+For+Chain+A'>AC1</scene> | ||
| - | |LIGAND= <scene name='pdbligand=ATP:ADENOSINE-5'-TRIPHOSPHATE'>ATP</scene> | + | |LIGAND= <scene name='pdbligand=5MU:5-METHYLURIDINE+5'-MONOPHOSPHATE'>5MU</scene>, <scene name='pdbligand=A:ADENOSINE-5'-MONOPHOSPHATE'>A</scene>, <scene name='pdbligand=ATP:ADENOSINE-5'-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=C:CYTIDINE-5'-MONOPHOSPHATE'>C</scene>, <scene name='pdbligand=G:GUANOSINE-5'-MONOPHOSPHATE'>G</scene>, <scene name='pdbligand=MAD:6-HYDRO-1-METHYLADENOSINE-5'-MONOPHOSPHATE'>MAD</scene>, <scene name='pdbligand=PSU:PSEUDOURIDINE-5'-MONOPHOSPHATE'>PSU</scene>, <scene name='pdbligand=TYB:TYROSINAL'>TYB</scene>, <scene name='pdbligand=U:URIDINE-5'-MONOPHOSPHATE'>U</scene> |
| - | |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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1h3e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h3e OCA], [http://www.ebi.ac.uk/pdbsum/1h3e PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1h3e RCSB]</span> | ||
}} | }} | ||
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[[Category: Tukalo, M.]] | [[Category: Tukalo, M.]] | ||
[[Category: Yaremchuk, A.]] | [[Category: Yaremchuk, A.]] | ||
| - | [[Category: ATP]] | ||
| - | [[Category: TYB]] | ||
[[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)]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:56:56 2008'' |
Revision as of 17:57, 30 March 2008
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| , resolution 2.90Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , , , , , , , , | ||||||
| Activity: | Tyrosine--tRNA ligase, with EC number 6.1.1.1 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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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