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.


2cuz

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2cuz.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:2cuz.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2cuz| PDB=2cuz | SCENE= }}
{{STRUCTURE_2cuz| PDB=2cuz | SCENE= }}
-
'''Glutamyl-tRNA synthetase from Thermus thermophilus in complex with L-glutamate'''
+
===Glutamyl-tRNA synthetase from Thermus thermophilus in complex with L-glutamate===
-
==Overview==
+
<!--
-
Glutamyl-tRNA synthetase (GluRS) is one of the aminoacyl-tRNA synthetases that require the cognate tRNA for specific amino acid recognition and activation. We analyzed the role of tRNA in amino acid recognition by crystallography. In the GluRS*tRNA(Glu)*Glu structure, GluRS and tRNA(Glu) collaborate to form a highly complementary L-glutamate-binding site. This collaborative site is functional, as it is formed in the same manner in pretransition-state mimic, GluRS*tRNA(Glu)*ATP*Eol (a glutamate analog), and posttransition-state mimic, GluRS*tRNA(Glu)*ESA (a glutamyl-adenylate analog) structures. In contrast, in the GluRS*Glu structure, only GluRS forms the amino acid-binding site, which is defective and accounts for the binding of incorrect amino acids, such as D-glutamate and L-glutamine. Therefore, tRNA(Glu) is essential for formation of the completely functional binding site for L-glutamate. These structures, together with our previously described structures, reveal that tRNA plays a crucial role in accurate positioning of both L-glutamate and ATP, thus driving the amino acid activation.
+
The line below this paragraph, {{ABSTRACT_PUBMED_17161369}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 17161369 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_17161369}}
==About this Structure==
==About this Structure==
Line 32: Line 36:
[[Category: Rsgi]]
[[Category: Rsgi]]
[[Category: Structural genomic]]
[[Category: Structural genomic]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 23:07:22 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 17:56:35 2008''

Revision as of 14:56, 27 July 2008

Image:2cuz.png

Template:STRUCTURE 2cuz

Glutamyl-tRNA synthetase from Thermus thermophilus in complex with L-glutamate

Template:ABSTRACT PUBMED 17161369

About this Structure

2CUZ is a Single protein structure of sequence from Thermus thermophilus. Full crystallographic information is available from OCA.

Reference

Structural bases of transfer RNA-dependent amino acid recognition and activation by glutamyl-tRNA synthetase., Sekine S, Shichiri M, Bernier S, Chenevert R, Lapointe J, Yokoyama S, Structure. 2006 Dec;14(12):1791-9. PMID:17161369

Page seeded by OCA on Sun Jul 27 17:56:35 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2cuz"
Personal tools