1wq4: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
No edit summary
OCA (talk | contribs)
No edit summary
Line 1: Line 1:
[[Image:1wq4.gif|left|200px]]
{{Seed}}
[[Image:1wq4.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1wq4|  PDB=1wq4  |  SCENE=  }}  
{{STRUCTURE_1wq4|  PDB=1wq4  |  SCENE=  }}  


'''Escherichia coli tyrosyl-tRNA synthetase mutant complexed with L-tyrosine'''
===Escherichia coli tyrosyl-tRNA synthetase mutant complexed with 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.
The line below this paragraph, {{ABSTRACT_PUBMED_15671170}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 15671170 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_15671170}}


==About this Structure==
==About this Structure==
Line 37: Line 41:
[[Category: Rsgi]]
[[Category: Rsgi]]
[[Category: Structural genomic]]
[[Category: Structural genomic]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 14:00:07 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 14:05:33 2008''

Revision as of 11:05, 27 July 2008

File:1wq4.png

Template:STRUCTURE 1wq4

Escherichia coli tyrosyl-tRNA synthetase mutant complexed with L-tyrosine

Template:ABSTRACT PUBMED 15671170

About this Structure

1WQ4 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 Sun Jul 27 14:05:33 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA