1vbn
From Proteopedia
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'''Escherichia coli tyrosyl-tRNA synthetase mutant complexed with Tyr-AMS''' | '''Escherichia coli tyrosyl-tRNA synthetase mutant complexed with Tyr-AMS''' | ||
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[[Category: Takimura, T.]] | [[Category: Takimura, T.]] | ||
[[Category: Yokoyama, S.]] | [[Category: Yokoyama, S.]] | ||
| - | [[Category: | + | [[Category: Ligase]] |
| - | [[Category: | + | [[Category: Riken structural genomics/proteomics initiative]] |
| - | [[Category: | + | [[Category: Rsgi]] |
| - | [[Category: | + | [[Category: Structural genomic]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 12:20:27 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 09:20, 3 May 2008
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 Page seeded by OCA on Sat May 3 12:20:27 2008
Categories: Escherichia coli | Single protein | Tyrosine--tRNA ligase | Kamata, K. | Kobayashi, T. | Nishimura, S. | RSGI, RIKEN Structural Genomics/Proteomics Initiative. | Sakamoto, K. | Sekine, R. | Takimura, T. | Yokoyama, S. | Ligase | Riken structural genomics/proteomics initiative | Rsgi | Structural genomic
