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1nyl

From Proteopedia

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{{STRUCTURE_1nyl| PDB=1nyl | SCENE= }}
{{STRUCTURE_1nyl| PDB=1nyl | SCENE= }}
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'''Unliganded glutaminyl-tRNA synthetase'''
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===Unliganded glutaminyl-tRNA synthetase===
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==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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(as it appears on PubMed at http://www.pubmed.gov), where 12737824 is the PubMed ID number.
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{{ABSTRACT_PUBMED_12737824}}
==About this Structure==
==About this Structure==
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[[Category: Sherlin, L D.]]
[[Category: Sherlin, L D.]]
[[Category: Ligase]]
[[Category: Ligase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 03:08:37 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 15:18:27 2008''

Revision as of 12:18, 27 July 2008

Image:1nyl.png

Template:STRUCTURE 1nyl

Unliganded glutaminyl-tRNA synthetase

Template:ABSTRACT PUBMED 12737824

About this Structure

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

Reference

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

Page seeded by OCA on Sun Jul 27 15:18:27 2008

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