This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1iq0

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1iq0.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1iq0.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1iq0| PDB=1iq0 | SCENE= }}
{{STRUCTURE_1iq0| PDB=1iq0 | SCENE= }}
-
'''THERMUS THERMOPHILUS ARGINYL-TRNA SYNTHETASE'''
+
===THERMUS THERMOPHILUS ARGINYL-TRNA SYNTHETASE===
-
==Overview==
+
<!--
-
Arginyl-tRNA synthetase (ArgRS) recognizes two major identity elements of tRNA(Arg): A20, located at the outside corner of the L-shaped tRNA, and C35, the second letter of the anticodon. Only a few exceptional organisms, such as the yeast Saccharomyces cerevisiae, lack A20 in tRNA(Arg). In the present study, we solved the crystal structure of a typical A20-recognizing ArgRS from Thermus thermophilus at 2.3 A resolution. The structure of the T. thermophilus ArgRS was found to be similar to that of the previously reported S. cerevisiae ArgRS, except for short insertions and a concomitant conformational change in the N-terminal domain. The structure of the yeast ArgRS.tRNA(Arg) complex suggested that two residues in the unique N-terminal domain, Tyr(77) and Asn(79), which are phylogenetically invariant in the ArgRSs from all organisms with A20 in tRNA(Arg)s, are involved in A20 recognition. However, in a docking model constructed based on the yeast ArgRS.tRNA(Arg) and T. thermophilus ArgRS structures, Tyr(77) and Asn(79) are not close enough to make direct contact with A20, because of the conformational change in the N-terminal domain. Nevertheless, the replacement of Tyr(77) or Asn(79) by Ala severely reduced the arginylation efficiency. Therefore, some conformational change around A20 is necessary for the recognition. Surprisingly, the N79D mutant equally recognized A20 and G20, with only a slight reduction in the arginylation efficiency as compared with the wild-type enzyme. Other mutants of Asn(79) also exhibited broader specificity for the nucleotide at position 20 of tRNA(Arg). We propose a model of A20 recognition by the ArgRS that is consistent with the present results of the mutational analyses.
+
The line below this paragraph, {{ABSTRACT_PUBMED_11698642}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 11698642 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_11698642}}
==About this Structure==
==About this Structure==
Line 33: Line 37:
[[Category: Rsgi]]
[[Category: Rsgi]]
[[Category: Structural genomic]]
[[Category: Structural genomic]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 20:16:08 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 13:47:19 2008''

Revision as of 10:47, 1 July 2008

Image:1iq0.png

Template:STRUCTURE 1iq0

THERMUS THERMOPHILUS ARGINYL-TRNA SYNTHETASE

Template:ABSTRACT PUBMED 11698642

About this Structure

1IQ0 is a Single protein structure of sequence from Thermus thermophilus. Full crystallographic information is available from OCA.

Reference

Structural and mutational studies of the recognition of the arginine tRNA-specific major identity element, A20, by arginyl-tRNA synthetase., Shimada A, Nureki O, Goto M, Takahashi S, Yokoyama S, Proc Natl Acad Sci U S A. 2001 Nov 20;98(24):13537-42. Epub 2001 Nov 6. PMID:11698642

Page seeded by OCA on Tue Jul 1 13:47:19 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1iq0"
Personal tools