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.


1qtq

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1qtq.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1qtq.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1qtq| PDB=1qtq | SCENE= }}
{{STRUCTURE_1qtq| PDB=1qtq | SCENE= }}
-
'''GLUTAMINYL-TRNA SYNTHETASE COMPLEXED WITH TRNA AND AN AMINO ACID ANALOG'''
+
===GLUTAMINYL-TRNA SYNTHETASE COMPLEXED WITH TRNA AND AN AMINO ACID ANALOG===
-
==Overview==
+
<!--
-
BACKGROUND: Aminoacyl-tRNA synthetases covalently link a specific amino acid to the correct tRNA. The fidelity of this reaction is essential for accurate protein synthesis. Each synthetase has a specific molecular mechanism to distinguish the correct pair of substrates from the pool of amino acids and isologous tRNA molecules. In the case of glutaminyl-tRNA synthetase (GlnRS) the prior binding of tRNA is required for activation of glutamine by ATP. A complete understanding of amino acid specificity in GlnRS requires the determination of the structure of the synthetase with both tRNA and substrates bound. RESULTS: A stable glutaminly-adenylate analog, which inhibits GlnRS with a Ki of 1.32 microM, was synthesized and cocrystallized with GlnRS and tRNA2Gln. The crystal structure of this ternary complex has been refined at 2.4 A resolution and shows the interactions made between glutamine and its binding site. CONCLUSIONS: To select against glutamic acid or glutamate, both hydrogen atoms of the nitrogen of the glutamine sidechain are recognized. The hydroxyl group of Tyr211 and a water molecule are responsible for this recognition; both are obligate hydrogen-bond acceptors due to a network of interacting sidechains and water molecules. The prior binding of tRNAGln that is required for amino acid activation may result from the terminal nucleotide, A76, packing against and orienting Tyr211, which forms part of the amino acid binding site.
+
The line below this paragraph, {{ABSTRACT_PUBMED_9562563}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 9562563 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_9562563}}
==About this Structure==
==About this Structure==
Line 33: Line 37:
[[Category: Trna synthetase]]
[[Category: Trna synthetase]]
[[Category: Trnagln]]
[[Category: Trnagln]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:41:42 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 16:02:12 2008''

Revision as of 13:02, 29 July 2008

Image:1qtq.png

Template:STRUCTURE 1qtq

GLUTAMINYL-TRNA SYNTHETASE COMPLEXED WITH TRNA AND AN AMINO ACID ANALOG

Template:ABSTRACT PUBMED 9562563

About this Structure

1QTQ is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

How glutaminyl-tRNA synthetase selects glutamine., Rath VL, Silvian LF, Beijer B, Sproat BS, Steitz TA, Structure. 1998 Apr 15;6(4):439-49. PMID:9562563

Page seeded by OCA on Tue Jul 29 16:02:12 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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