1g51

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[[Image:1g51.jpg|left|200px]]
[[Image:1g51.jpg|left|200px]]
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{{Structure
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|PDB= 1g51 |SIZE=350|CAPTION= <scene name='initialview01'>1g51</scene>, resolution 2.40&Aring;
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The line below this paragraph, containing "STRUCTURE_1g51", creates the "Structure Box" on the page.
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|SITE=
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|LIGAND= <scene name='pdbligand=AMO:ASPARTYL-ADENOSINE-5&#39;-MONOPHOSPHATE'>AMO</scene>, <scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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|GENE=
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|DOMAIN=
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{{STRUCTURE_1g51| PDB=1g51 | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1g51 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g51 OCA], [http://www.ebi.ac.uk/pdbsum/1g51 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1g51 RCSB]</span>
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'''ASPARTYL TRNA SYNTHETASE FROM THERMUS THERMOPHILUS AT 2.4 A RESOLUTION'''
'''ASPARTYL TRNA SYNTHETASE FROM THERMUS THERMOPHILUS AT 2.4 A RESOLUTION'''
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[[Category: Poterzsman, A.]]
[[Category: Poterzsman, A.]]
[[Category: Thierry, J C.]]
[[Category: Thierry, J C.]]
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[[Category: aminoacyl trna synthetase]]
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[[Category: Aminoacyl trna synthetase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 17:08:48 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:36:49 2008''
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Revision as of 14:08, 2 May 2008

Image:1g51.jpg

Template:STRUCTURE 1g51

ASPARTYL TRNA SYNTHETASE FROM THERMUS THERMOPHILUS AT 2.4 A RESOLUTION


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.

About this Structure

1G51 is a Single protein structure of sequence from Thermus thermophilus. Full crystallographic information is available from OCA.

Reference

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 Fri May 2 17:08:48 2008

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