1wq3

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|SITE=
|SITE=
|LIGAND= <scene name='pdbligand=IYR:3-IODO-TYROSINE'>IYR</scene>
|LIGAND= <scene name='pdbligand=IYR:3-IODO-TYROSINE'>IYR</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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|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= tyrS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
|GENE= tyrS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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|DOMAIN=
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|RELATEDENTRY=[[1wq4|1WQ4]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1wq3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wq3 OCA], [http://www.ebi.ac.uk/pdbsum/1wq3 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1wq3 RCSB]</span>
}}
}}
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[[Category: Takimura, T.]]
[[Category: Takimura, T.]]
[[Category: Yokoyama, S.]]
[[Category: Yokoyama, S.]]
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[[Category: IYR]]
 
[[Category: aminoacyl-trna sybthetase]]
[[Category: aminoacyl-trna sybthetase]]
[[Category: ligase]]
[[Category: ligase]]
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[[Category: structural genomic]]
[[Category: structural genomic]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:00:09 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:39:33 2008''

Revision as of 21:39, 30 March 2008

Image:1wq3.gif


PDB ID 1wq3

Drag the structure with the mouse to rotate
, resolution 2.00Å
Ligands:
Gene: tyrS (Escherichia coli)
Activity: Tyrosine--tRNA ligase, with EC number 6.1.1.1
Related: 1WQ4


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Escherichia coli tyrosyl-tRNA synthetase mutant comlexed with 3-iodo-L-tyrosine


Overview

The genetic code in a eukaryotic system has been expanded by the engineering of Escherichia coli tyrosyl-tRNA synthetase (TyrRS) with the Y37V and Q195C mutations (37V195C), which specifically recognize 3-iodo-L-tyrosine rather than L-tyrosine. In the present study, we determined the 3-iodo-L-tyrosine- and L-tyrosine-bound structures of the 37V195C mutant of the E. coli TyrRS catalytic domain at 2.0-A resolution. The gamma-methyl group of Val-37 and the sulfur atom of Cys-195 make van der Waals contacts with the iodine atom of 3-iodo-L-tyrosine. The Val-37 and Cys-195 side chains are rigidly fixed by the neighboring residues forming the hydrophobic core of the TyrRS. The major roles of the two mutations are different for the 3-iodo-L-tyrosine-selective recognition in the first step of the aminoacylation reaction (the amino acid activation step): the Y37V mutation eliminates the fatal steric repulsion with the iodine atom, and the Q195C mutation reduces the L-tyrosine misrecognition. The structure of the 37V195C mutant TyrRS complexed with an L-tyrosyladenylate analogue was also solved, indicating that the 3-iodo-L-tyrosine and L-tyrosine side chains are similarly discriminated in the second step (the aminoacyl transfer step). These results demonstrate that the amino acid-binding pocket on the 37V195C mutant is optimized for specific 3-iodo-L-tyrosine recognition.

About this Structure

1WQ3 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Structural basis of nonnatural amino acid recognition by an engineered aminoacyl-tRNA synthetase for genetic code expansion., Kobayashi T, Sakamoto K, Takimura T, Sekine R, Kelly VP, Kamata K, Nishimura S, Yokoyama S, Proc Natl Acad Sci U S A. 2005 Feb 1;102(5):1366-71. Epub 2005 Jan 25. PMID:15671170

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