2amc: Difference between revisions

Revision as of 13:11, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2amc.png

Template:STRUCTURE 2amc

Crystal structure of Phenylalanyl-tRNA synthetase complexed with L-tyrosineCrystal structure of Phenylalanyl-tRNA synthetase complexed with L-tyrosine

Template:ABSTRACT PUBMED 16338408

About this StructureAbout this Structure

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

ReferenceReference

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 13:11:51 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:2amc.gif|left|200px]]
+{{Seed}}
+[[Image:2amc.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_2amc|  PDB=2amc  |  SCENE=  }}
-'''Crystal structure of Phenylalanyl-tRNA synthetase complexed with L-tyrosine'''
+===Crystal structure of Phenylalanyl-tRNA synthetase complexed with L-tyrosine===
-==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==
@@ Line 28: / Line 32: @@
 [[Category: Tworowski, D.]]
 [[Category: Protein-amino acid complex]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 19:12:49 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 13:11:51 2008''