1vbn: Difference between revisions
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[[Image:1vbn.gif|left|200px]] | [[Image:1vbn.gif|left|200px]] | ||
'''Escherichia coli tyrosyl-tRNA synthetase mutant complexed with Tyr-AMS''' | {{Structure | ||
|PDB= 1vbn |SIZE=350|CAPTION= <scene name='initialview01'>1vbn</scene>, resolution 2.70Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=YSA:5'-O-[N-(L-TYROSYL)SULFAMOYL]ADENOSINE'>YSA</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] | |||
|GENE= | |||
}} | |||
'''Escherichia coli tyrosyl-tRNA synthetase mutant complexed with Tyr-AMS''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1VBN is a [ | 1VBN is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VBN OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15671170 15671170] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: riken structural genomics/proteomics initiative]] | [[Category: riken structural genomics/proteomics initiative]] | ||
[[Category: rsgi]] | [[Category: rsgi]] | ||
[[Category: structural | [[Category: structural genomic]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:43:32 2008'' | ||
Revision as of 12:43, 20 March 2008
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| 1vbn, resolution 2.70Å | |||||||||||||
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| Ligands: | YSA | ||||||||||||
| Activity: | Tyrosine--tRNA ligase, with EC number 6.1.1.1 | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
Escherichia coli tyrosyl-tRNA synthetase mutant complexed with Tyr-AMS
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
1VBN 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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