1g51: Difference between revisions

Revision as of 13:46, 21 February 2008

ASPARTYL TRNA SYNTHETASE FROM THERMUS THERMOPHILUS AT 2.4 A RESOLUTION

OverviewOverview

The crystal structures of Thermus thermophilus aspartyl-tRNA synthetase and of its complex with ATP, Mg2+ and aspartic acid, show in situ formation of the amino acid adenylate and furnish experimental evidence for the modes of recognition of aspartic acid and ATP. The amino acid fits in a predefined specific site in which it replaces water molecules without significant conformational changes of the binding residues. This mode of selection is reminiscent of the lock and key concept. The pocket is closed by the movement of a histidine side chain from a neighbouring loop acting as a valve. ATP binding is driven by the stacking of the adenine upon the otherwise fixed aromatic ring of the class-II-invariant phenylalanine Phe235. Specific recognition is achieved by interactions with the flexible side chains of other class-II-conserved residues. Conformational changes have been identified which allow the description of a reaction pathway including both lock-and-key and induced-fit interactions. This pathway can presumably be extended to all class II aaRS.

About this StructureAbout this Structure

1G51 is a Single protein structure of sequence from Thermus thermophilus with , and as ligands. Active as Aspartate--tRNA ligase, with EC number 6.1.1.12 Full crystallographic information is available from OCA.

ReferenceReference

Synthesis and recognition of aspartyl-adenylate by Thermus thermophilus aspartyl-tRNA synthetase., Poterszman A, Delarue M, Thierry JC, Moras D, J Mol Biol. 1994 Nov 25;244(2):158-67. PMID:7966328

Page seeded by OCA on Thu Feb 21 12:46:13 2008

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OCA

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-[[Image:1g51.jpg|left|200px]]<br /><applet load="1g51" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1g51.jpg|left|200px]]<br /><applet load="1g51" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1g51, resolution 2.40&Aring;" />
 '''ASPARTYL TRNA SYNTHETASE FROM THERMUS THERMOPHILUS AT 2.4 A RESOLUTION'''<br />
 ==Overview==
-The crystal structures of Thermus thermophilus aspartyl-tRNA synthetase, and of its complex with ATP, Mg2+ and aspartic acid, show in situ, formation of the amino acid adenylate and furnish experimental evidence, for the modes of recognition of aspartic acid and ATP. The amino acid fits, in a predefined specific site in which it replaces water molecules without, significant conformational changes of the binding residues. This mode of, selection is reminiscent of the lock and key concept. The pocket is closed, by the movement of a histidine side chain from a neighbouring loop acting, as a valve. ATP binding is driven by the stacking of the adenine upon the, otherwise fixed aromatic ring of the class-II-invariant phenylalanine, Phe235. Specific recognition is achieved by interactions with the flexible, side chains of other class-II-conserved residues. Conformational changes, have been identified which allow the description of a reaction pathway, including both lock-and-key and induced-fit interactions. This pathway can, presumably be extended to all class II aaRS.
+The crystal structures of Thermus thermophilus aspartyl-tRNA synthetase and of its complex with ATP, Mg2+ and aspartic acid, show in situ formation of the amino acid adenylate and furnish experimental evidence for the modes of recognition of aspartic acid and ATP. The amino acid fits in a predefined specific site in which it replaces water molecules without significant conformational changes of the binding residues. This mode of selection is reminiscent of the lock and key concept. The pocket is closed by the movement of a histidine side chain from a neighbouring loop acting as a valve. ATP binding is driven by the stacking of the adenine upon the otherwise fixed aromatic ring of the class-II-invariant phenylalanine Phe235. Specific recognition is achieved by interactions with the flexible side chains of other class-II-conserved residues. Conformational changes have been identified which allow the description of a reaction pathway including both lock-and-key and induced-fit interactions. This pathway can presumably be extended to all class II aaRS.
 ==About this Structure==
-G51 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus] with SO4, AMO and AMP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Aspartate--tRNA_ligase Aspartate--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.12 6.1.1.12] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1G51 OCA].
+G51 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus] with <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=AMO:'>AMO</scene> and <scene name='pdbligand=AMP:'>AMP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Aspartate--tRNA_ligase Aspartate--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.12 6.1.1.12] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G51 OCA].
 ==Reference==
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 [[Category: Moras, D.]]
 [[Category: Poterzsman, A.]]
-[[Category: Thierry, J.C.]]
+[[Category: Thierry, J C.]]
 [[Category: AMO]]
 [[Category: AMP]]
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 [[Category: aminoacyl trna synthetase]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:42:48 2007''
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