1vbn

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1vbn.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1vbn.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1vbn| PDB=1vbn | SCENE= }}
{{STRUCTURE_1vbn| PDB=1vbn | SCENE= }}
-
'''Escherichia coli tyrosyl-tRNA synthetase mutant complexed with Tyr-AMS'''
+
===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.
+
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 35: Line 39:
[[Category: Rsgi]]
[[Category: Rsgi]]
[[Category: Structural genomic]]
[[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 Mon Jul 28 06:09:18 2008''

Revision as of 03:09, 28 July 2008

Image:1vbn.png

Template:STRUCTURE 1vbn

Escherichia coli tyrosyl-tRNA synthetase mutant complexed with Tyr-AMS

Template:ABSTRACT PUBMED 15671170

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 Mon Jul 28 06:09:18 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1vbn"
Personal tools