1nyl: Difference between revisions

Revision as of 15:18, 27 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:1nyl.png

Template:STRUCTURE 1nyl

Unliganded glutaminyl-tRNA synthetaseUnliganded glutaminyl-tRNA synthetase

Template:ABSTRACT PUBMED 12737824

About this StructureAbout this Structure

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

ReferenceReference

tRNA-dependent active site assembly in a class I aminoacyl-tRNA synthetase., Sherlin LD, Perona JJ, Structure. 2003 May;11(5):591-603. PMID:12737824

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OCA

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-'''Unliganded glutaminyl-tRNA synthetase'''
+===Unliganded glutaminyl-tRNA synthetase===
-==Overview==
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-The crystal structure of ligand-free E. coli glutaminyl-tRNA synthetase (GlnRS) at 2.4 A resolution shows that substrate binding is essential to construction of a catalytically proficient active site. tRNA binding generates structural changes throughout the enzyme, repositioning key active site peptides that bind glutamine and ATP. The structure gives insight into longstanding questions regarding the tRNA dependence of glutaminyl adenylate formation, the coupling of amino acid and tRNA selectivities, and the roles of specific pathways for transmission of tRNA binding signals to the active site. Comparative analysis of the unliganded and tRNA-bound structures shows, in detail, how flexibility is built into the enzyme architecture and suggests that the induced-fit transitions are a key underlying determinant of both amino acid and tRNA specificity.
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 ==About this Structure==
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 [[Category: Sherlin, L D.]]
 [[Category: Ligase]]
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