1b8a

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[[Image:1b8a.gif|left|200px]]
[[Image:1b8a.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1b8a |SIZE=350|CAPTION= <scene name='initialview01'>1b8a</scene>, resolution 1.90&Aring;
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The line below this paragraph, containing "STRUCTURE_1b8a", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=ATP:ADENOSINE-5&#39;-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</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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or leave the SCENE parameter empty for the default display.
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|GENE= ASPS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=311400 Thermococcus kodakarensis])
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-->
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|DOMAIN=
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{{STRUCTURE_1b8a| PDB=1b8a | 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=1b8a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b8a OCA], [http://www.ebi.ac.uk/pdbsum/1b8a PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1b8a RCSB]</span>
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}}
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'''ASPARTYL-TRNA SYNTHETASE'''
'''ASPARTYL-TRNA SYNTHETASE'''
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[[Category: Schmitt, E.]]
[[Category: Schmitt, E.]]
[[Category: Thierry, J C.]]
[[Category: Thierry, J C.]]
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[[Category: synthetase]]
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[[Category: Synthetase]]
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[[Category: trna ligase,]]
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[[Category: Trna ligase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 11:11:45 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:55:38 2008''
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Revision as of 08:11, 2 May 2008

Image:1b8a.gif

Template:STRUCTURE 1b8a

ASPARTYL-TRNA SYNTHETASE


Overview

The crystal structure of aspartyl-tRNA synthetase (AspRS) from Pyrococcus kodakaraensis was solved at 1.9 A resolution. The sequence and three-dimensional structure of the catalytic domain are highly homologous to those of eukaryotic AspRSs. In contrast, the N-terminal domain, whose function is to bind the tRNA anticodon, is more similar to that of eubacterial enzymes. Its structure explains the unique property of archaeal AspRSs of accommodating both tRNAAsp and tRNAAsn. Soaking the apo-enzyme crystals with ATP and aspartic acid both separately and together allows the adenylate formation to be followed. Due to the asymmetry of the dimeric enzyme in the crystalline state, different steps of the reaction could be visualized within the same crystal. Four different states of the aspartic acid activation reaction could thus be characterized, revealing the functional correlation of the observed conformational changes. The binding of the amino acid substrate induces movement of two invariant loops which secure the position of the peptidyl moiety for adenylate formation. An unambiguous spatial and functional assignment of three magnesium ion cofactors can be made. This study shows the important role of residues present in both archaeal and eukaryotic AspRSs, but absent from the eubacterial enzymes.

About this Structure

1B8A is a Single protein structure of sequence from Thermococcus kodakarensis. Full crystallographic information is available from OCA.

Reference

Crystal structure of aspartyl-tRNA synthetase from Pyrococcus kodakaraensis KOD: archaeon specificity and catalytic mechanism of adenylate formation., Schmitt E, Moulinier L, Fujiwara S, Imanaka T, Thierry JC, Moras D, EMBO J. 1998 Sep 1;17(17):5227-37. PMID:9724658 Page seeded by OCA on Fri May 2 11:11:45 2008

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