1f7v: Difference between revisions

Revision as of 13:35, 21 February 2008

CRYSTAL STRUCTURE OF YEAST ARGINYL-TRNA SYNTHETASE COMPLEXED WITH THE TRNAARG

OverviewOverview

The 2.2 A crystal structure of a ternary complex formed by yeast arginyl-tRNA synthetase and its cognate tRNA(Arg) in the presence of the L-arginine substrate highlights new atomic features used for specific substrate recognition. This first example of an active complex formed by a class Ia aminoacyl-tRNA synthetase and its natural cognate tRNA illustrates additional strategies used for specific tRNA selection. The enzyme specifically recognizes the D-loop and the anticodon of the tRNA, and the mutually induced fit produces a conformation of the anticodon loop never seen before. Moreover, the anticodon binding triggers conformational changes in the catalytic center of the protein. The comparison with the 2.9 A structure of a binary complex formed by yeast arginyl-tRNA synthetase and tRNA(Arg) reveals that L-arginine binding controls the correct positioning of the CCA end of the tRNA(Arg). Important structural changes induced by substrate binding are observed in the enzyme. Several key residues of the active site play multiple roles in the catalytic pathway and thus highlight the structural dynamics of the aminoacylation reaction.

About this StructureAbout this Structure

1F7V is a Single protein structure of sequence from Saccharomyces servazzii. Active as Arginine--tRNA ligase, with EC number 6.1.1.19 Full crystallographic information is available from OCA.

ReferenceReference

tRNA aminoacylation by arginyl-tRNA synthetase: induced conformations during substrates binding., Delagoutte B, Moras D, Cavarelli J, EMBO J. 2000 Nov 1;19(21):5599-610. PMID:11060012

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-[[Image:1f7v.jpg|left|200px]]<br /><applet load="1f7v" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1f7v.jpg|left|200px]]<br /><applet load="1f7v" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1f7v, resolution 2.90&Aring;" />
 '''CRYSTAL STRUCTURE OF YEAST ARGINYL-TRNA SYNTHETASE COMPLEXED WITH THE TRNAARG'''<br />
 ==Overview==
-The 2.2 A crystal structure of a ternary complex formed by yeast, arginyl-tRNA synthetase and its cognate tRNA(Arg) in the presence of the, L-arginine substrate highlights new atomic features used for specific, substrate recognition. This first example of an active complex formed by a, class Ia aminoacyl-tRNA synthetase and its natural cognate tRNA, illustrates additional strategies used for specific tRNA selection. The, enzyme specifically recognizes the D-loop and the anticodon of the tRNA, and the mutually induced fit produces a conformation of the anticodon loop, never seen before. Moreover, the anticodon binding triggers conformational, changes in the catalytic center of the protein. The comparison with the, 2.9 A structure of a binary complex formed by yeast arginyl-tRNA, synthetase and tRNA(Arg) reveals that L-arginine binding controls the, correct positioning of the CCA end of the tRNA(Arg). Important structural, changes induced by substrate binding are observed in the enzyme. Several, key residues of the active site play multiple roles in the catalytic, pathway and thus highlight the structural dynamics of the aminoacylation, reaction.
+The 2.2 A crystal structure of a ternary complex formed by yeast arginyl-tRNA synthetase and its cognate tRNA(Arg) in the presence of the L-arginine substrate highlights new atomic features used for specific substrate recognition. This first example of an active complex formed by a class Ia aminoacyl-tRNA synthetase and its natural cognate tRNA illustrates additional strategies used for specific tRNA selection. The enzyme specifically recognizes the D-loop and the anticodon of the tRNA, and the mutually induced fit produces a conformation of the anticodon loop never seen before. Moreover, the anticodon binding triggers conformational changes in the catalytic center of the protein. The comparison with the 2.9 A structure of a binary complex formed by yeast arginyl-tRNA synthetase and tRNA(Arg) reveals that L-arginine binding controls the correct positioning of the CCA end of the tRNA(Arg). Important structural changes induced by substrate binding are observed in the enzyme. Several key residues of the active site play multiple roles in the catalytic pathway and thus highlight the structural dynamics of the aminoacylation reaction.
 ==About this Structure==
-F7V is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_servazzii Saccharomyces servazzii]. Active as [http://en.wikipedia.org/wiki/Arginine--tRNA_ligase Arginine--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.19 6.1.1.19] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1F7V OCA].
+F7V is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_servazzii Saccharomyces servazzii]. Active as [http://en.wikipedia.org/wiki/Arginine--tRNA_ligase Arginine--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.19 6.1.1.19] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F7V OCA].
 ==Reference==
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 [[Category: trna-protein complex]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:41:21 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:35:52 2008''