1wka

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1wka.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1wka.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1wka| PDB=1wka | SCENE= }}
{{STRUCTURE_1wka| PDB=1wka | SCENE= }}
-
'''Structural basis for non-cognate amino acid discrimination by the valyl-tRNA synthetase editing domain'''
+
===Structural basis for non-cognate amino acid discrimination by the valyl-tRNA synthetase editing domain===
-
==Overview==
+
<!--
-
The editing domain of valyl-tRNA synthetase (ValRS) is known to deacylate, or edit, misformed Thr-tRNA(Val) (post-transfer editing). Here, we determined the 1.7-Angstroms resolution crystal structure of the Thermus thermophilus ValRS editing domain. A comparison of the structure with the previously reported tRNA complex structure revealed conformational changes of the editing domain upon accommodation of the terminal A76; the "GTG loop" moves to expand the pocket, and the side chain of Phe-264 on the GTG loop rotates to interact with the A76 adenine ring. If these conformational changes did not occur, then C75 and A76 of the tRNA would clash with Phe-264. To elucidate the mechanism of the threonine side-chain recognition, we determined the crystal structure of the editing domain bound with [N-(L-threonyl)-sulfamoyl]adenosine at 1.7-Angstroms resolution. The gamma-OH of the threonyl moiety is recognized by the Lys-270, Thr-272, and Asp-279 side chains, which may reject the cognate valyl moiety. Accordingly, ValRS mutants with an Ala substitution for Lys-270 or Asp-279 synthesized significant amounts of Thr-tRNA(Val). The misproduced Thr-tRNA(Val) was hydrolyzed efficiently by the wild-type ValRS, but this post-transfer editing activity was drastically impaired by the Ala substitutions for Lys-270 and Asp-279 and was also decreased by those for Arg-216, Phe-264, and Thr-272. These results indicate that the threonyl moiety and A76 of Thr-tRNA(Val) are recognized by the Lys-270, Thr-272, and Asp-279 side chains and by the Phe-264 side chain, respectively, of the ValRS editing domain.
+
The line below this paragraph, {{ABSTRACT_PUBMED_15970591}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 15970591 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_15970591}}
==About this Structure==
==About this Structure==
Line 36: Line 40:
[[Category: Translation]]
[[Category: Translation]]
[[Category: Valyl-trna synthetase]]
[[Category: Valyl-trna synthetase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 13:47:41 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 09:59:19 2008''

Revision as of 06:59, 29 July 2008

Template:STRUCTURE 1wka

Structural basis for non-cognate amino acid discrimination by the valyl-tRNA synthetase editing domain

Template:ABSTRACT PUBMED 15970591

About this Structure

1WKA is a Single protein structure of sequence from Thermus thermophilus. Full crystallographic information is available from OCA.

Reference

Structural basis for non-cognate amino acid discrimination by the valyl-tRNA synthetase editing domain., Fukunaga R, Yokoyama S, J Biol Chem. 2005 Aug 19;280(33):29937-45. Epub 2005 Jun 21. PMID:15970591

Page seeded by OCA on Tue Jul 29 09:59:19 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools