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.


2akw

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2akw.gif|left|200px]]
+
{{Seed}}
 +
[[Image:2akw.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2akw| PDB=2akw | SCENE= }}
{{STRUCTURE_2akw| PDB=2akw | SCENE= }}
-
'''Crystal Structure of T.Thermophilus Phenylalanyl-tRNA synthetase complexed with p-Cl-Phenylalanine'''
+
===Crystal Structure of T.Thermophilus Phenylalanyl-tRNA synthetase complexed with p-Cl-Phenylalanine===
-
==Overview==
+
<!--
-
Aminoacyl-tRNA synthetases (aaRSs) exert control over the faithful transfer of amino acids onto cognate tRNAs. Since chemical structures of various amino acids closely resemble each other, it is difficult to discriminate between them. Editing activity has been evolved by certain aaRSs to resolve the problem. In this study, we determined the crystal structures of complexes of T. thermophilus phenylalanyl-tRNA synthetase (PheRS) with L-tyrosine, p-chloro-phenylalanine, and a nonhydrolyzable tyrosyl-adenylate analog. The structures demonstrate plasticity of the synthetic site capable of binding substrates larger than phenylalanine and provide a structural basis for the proofreading mechanism. The editing site is localized at the B3/B4 interface, 35 A from the synthetic site. Glubeta334 plays a crucial role in the specific recognition of the Tyr moiety in the editing site. The tyrosyl-adenylate analog binds exclusively in the synthetic site. Both structural data and tyrosine-dependent ATP hydrolysis enhanced by tRNA(Phe) provide evidence for a preferential posttransfer editing pathway in the phenylalanine-specific system.
+
The line below this paragraph, {{ABSTRACT_PUBMED_16338408}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 16338408 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_16338408}}
==About this Structure==
==About this Structure==
Line 28: Line 32:
[[Category: Tworowski, D E.]]
[[Category: Tworowski, D E.]]
[[Category: Protein-unnatural amino acid complex]]
[[Category: Protein-unnatural amino acid complex]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 19:10:24 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 03:05:42 2008''

Revision as of 00:05, 28 July 2008

Image:2akw.png

Template:STRUCTURE 2akw

Crystal Structure of T.Thermophilus Phenylalanyl-tRNA synthetase complexed with p-Cl-Phenylalanine

Template:ABSTRACT PUBMED 16338408

About this Structure

2AKW is a Protein complex structure of sequences from Thermus thermophilus. Full crystallographic information is available from OCA.

Reference

Structural basis for discrimination of L-phenylalanine from L-tyrosine by phenylalanyl-tRNA synthetase., Kotik-Kogan O, Moor N, Tworowski D, Safro M, Structure. 2005 Dec;13(12):1799-807. PMID:16338408

Page seeded by OCA on Mon Jul 28 03:05:42 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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