1nyl: Difference between revisions

Revision as of 15:11, 21 February 2008

Unliganded glutaminyl-tRNA synthetase

OverviewOverview

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.

About this StructureAbout this Structure

1NYL is a Single protein structure of sequence from Escherichia coli. Active as Glutamine--tRNA ligase, with EC number 6.1.1.18 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

Page seeded by OCA on Thu Feb 21 14:11:30 2008

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

OCA

@@ Line 1: / Line 1: @@
-[[Image:1nyl.jpg|left|200px]]<br /><applet load="1nyl" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1nyl.jpg|left|200px]]<br /><applet load="1nyl" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1nyl, resolution 2.60&Aring;" />
 '''Unliganded glutaminyl-tRNA synthetase'''<br />
 ==Overview==
-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.
+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.
 ==About this Structure==
-NYL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Active as [http://en.wikipedia.org/wiki/Glutamine--tRNA_ligase Glutamine--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.18 6.1.1.18] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1NYL OCA].
+NYL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Active as [http://en.wikipedia.org/wiki/Glutamine--tRNA_ligase Glutamine--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.18 6.1.1.18] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NYL OCA].
 ==Reference==
@@ Line 14: / Line 14: @@
 [[Category: Glutamine--tRNA ligase]]
 [[Category: Single protein]]
-[[Category: Perona, J.P.]]
+[[Category: Perona, J P.]]
-[[Category: Sherlin, L.D.]]
+[[Category: Sherlin, L D.]]
 [[Category: ligase]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 22:39:49 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:11:30 2008''