1qf6: Difference between revisions

Revision as of 15:38, 21 February 2008

STRUCTURE OF E. COLI THREONYL-TRNA SYNTHETASE COMPLEXED WITH ITS COGNATE TRNA

OverviewOverview

E. coli threonyl-tRNA synthetase (ThrRS) is a class II enzyme that represses the translation of its own mRNA. We report the crystal structure at 2.9 A resolution of the complex between tRNA(Thr) and ThrRS, whose structural features reveal novel strategies for providing specificity in tRNA selection. These include an amino-terminal domain containing a novel protein fold that makes minor groove contacts with the tRNA acceptor stem. The enzyme induces a large deformation of the anticodon loop, resulting in an interaction between two adjacent anticodon bases, which accounts for their prominent role in tRNA identity and translational regulation. A zinc ion found in the active site is implicated in amino acid recognition/discrimination.

About this StructureAbout this Structure

1QF6 is a Single protein structure of sequence from Escherichia coli with and as ligands. The following page contains interesting information on the relation of 1QF6 with [Aminoacyl-tRNA Synthetases]. Active as Threonine--tRNA ligase, with EC number 6.1.1.3 Full crystallographic information is available from OCA.

ReferenceReference

The structure of threonyl-tRNA synthetase-tRNA(Thr) complex enlightens its repressor activity and reveals an essential zinc ion in the active site., Sankaranarayanan R, Dock-Bregeon AC, Romby P, Caillet J, Springer M, Rees B, Ehresmann C, Ehresmann B, Moras D, Cell. 1999 Apr 30;97(3):371-81. PMID:10319817

Page seeded by OCA on Thu Feb 21 14:38:50 2008

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

OCA

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-[[Image:1qf6.gif|left|200px]]<br />
+[[Image:1qf6.gif|left|200px]]<br /><applet load="1qf6" size="350" color="white" frame="true" align="right" spinBox="true"
-<applet load="1qf6" size="450" color="white" frame="true" align="right" spinBox="true"
 caption="1qf6, resolution 2.9&Aring;" />
 '''STRUCTURE OF E. COLI THREONYL-TRNA SYNTHETASE COMPLEXED WITH ITS COGNATE TRNA'''<br />
 ==Overview==
-E. coli threonyl-tRNA synthetase (ThrRS) is a class II enzyme that, represses the translation of its own mRNA. We report the crystal structure, at 2.9 A resolution of the complex between tRNA(Thr) and ThrRS, whose, structural features reveal novel strategies for providing specificity in, tRNA selection. These include an amino-terminal domain containing a novel, protein fold that makes minor groove contacts with the tRNA acceptor stem., The enzyme induces a large deformation of the anticodon loop, resulting in, an interaction between two adjacent anticodon bases, which accounts for, their prominent role in tRNA identity and translational regulation. A zinc, ion found in the active site is implicated in amino acid, recognition/discrimination.
+E. coli threonyl-tRNA synthetase (ThrRS) is a class II enzyme that represses the translation of its own mRNA. We report the crystal structure at 2.9 A resolution of the complex between tRNA(Thr) and ThrRS, whose structural features reveal novel strategies for providing specificity in tRNA selection. These include an amino-terminal domain containing a novel protein fold that makes minor groove contacts with the tRNA acceptor stem. The enzyme induces a large deformation of the anticodon loop, resulting in an interaction between two adjacent anticodon bases, which accounts for their prominent role in tRNA identity and translational regulation. A zinc ion found in the active site is implicated in amino acid recognition/discrimination.
 ==About this Structure==
-QF6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with ZN and AMP as [http://en.wikipedia.org/wiki/ligands ligands]. The following page contains interesting information on the relation of 1QF6 with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb16_1.html Aminoacyl-tRNA Synthetases]]. Active as [http://en.wikipedia.org/wiki/Threonine--tRNA_ligase Threonine--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.3 6.1.1.3] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1QF6 OCA].
+QF6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=AMP:'>AMP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. The following page contains interesting information on the relation of 1QF6 with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb16_1.html Aminoacyl-tRNA Synthetases]]. Active as [http://en.wikipedia.org/wiki/Threonine--tRNA_ligase Threonine--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.3 6.1.1.3] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QF6 OCA].
 ==Reference==
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 [[Category: Single protein]]
 [[Category: Threonine--tRNA ligase]]
-[[Category: Dock-Bregeon, A.C.]]
+[[Category: Dock-Bregeon, A C.]]
 [[Category: Moras, D.]]
 [[Category: Rees, B.]]
@@ Line 31: / Line 30: @@
 [[Category: zinc]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 18 09:05:04 2007''
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