1efw

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[[Image:1efw.gif|left|200px]]
[[Image:1efw.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1efw |SIZE=350|CAPTION= <scene name='initialview01'>1efw</scene>, resolution 3.00&Aring;
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The line below this paragraph, containing "STRUCTURE_1efw", 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=2MA:2-METHYLADENOSINE-5&#39;-MONOPHOSPHATE'>2MA</scene>, <scene name='pdbligand=4SU:4-THIOURIDINE-5&#39;-MONOPHOSPHATE'>4SU</scene>, <scene name='pdbligand=5MU:5-METHYLURIDINE+5&#39;-MONOPHOSPHATE'>5MU</scene>, <scene name='pdbligand=A:ADENOSINE-5&#39;-MONOPHOSPHATE'>A</scene>, <scene name='pdbligand=C:CYTIDINE-5&#39;-MONOPHOSPHATE'>C</scene>, <scene name='pdbligand=G:GUANOSINE-5&#39;-MONOPHOSPHATE'>G</scene>, <scene name='pdbligand=G7M:N7-METHYL-GUANOSINE-5&#39;-MONOPHOSPHATE'>G7M</scene>, <scene name='pdbligand=H2U:5,6-DIHYDROURIDINE-5&#39;-MONOPHOSPHATE'>H2U</scene>, <scene name='pdbligand=PSU:PSEUDOURIDINE-5&#39;-MONOPHOSPHATE'>PSU</scene>, <scene name='pdbligand=QUO:2-AMINO-7-DEAZA-(2&#39;&#39;,3&#39;&#39;-DIHYDROXY-CYCLOPENTYLAMINO)-GUANOSINE-5&#39;-MONOPHOSPHATE'>QUO</scene>, <scene name='pdbligand=T:THYMIDINE-5&#39;-MONOPHOSPHATE'>T</scene>, <scene name='pdbligand=U:URIDINE-5&#39;-MONOPHOSPHATE'>U</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=
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|DOMAIN=
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{{STRUCTURE_1efw| PDB=1efw | 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=1efw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1efw OCA], [http://www.ebi.ac.uk/pdbsum/1efw PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1efw RCSB]</span>
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}}
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'''CRYSTAL STRUCTURE OF ASPARTYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS COMPLEXED TO TRNAASP FROM ESCHERICHIA COLI'''
'''CRYSTAL STRUCTURE OF ASPARTYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS COMPLEXED TO TRNAASP FROM ESCHERICHIA COLI'''
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[[Category: Thierry, J C.]]
[[Category: Thierry, J C.]]
[[Category: Webster, G.]]
[[Category: Webster, G.]]
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[[Category: aspartyl-trna synthetase]]
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[[Category: Aspartyl-trna synthetase]]
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[[Category: ligase/rna]]
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[[Category: Ligase/rna]]
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[[Category: protein/rna complex]]
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[[Category: Protein/rna complex]]
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[[Category: trna]]
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[[Category: Trna]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:02:52 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:01:49 2008''
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Revision as of 12:02, 2 May 2008

Template:STRUCTURE 1efw

CRYSTAL STRUCTURE OF ASPARTYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS COMPLEXED TO TRNAASP FROM ESCHERICHIA COLI


Overview

The crystal structures of aspartyl-tRNA synthetase (AspRS) from Thermus thermophilus, a prokaryotic class IIb enzyme, complexed with tRNA(Asp) from either T. thermophilus or Escherichia coli reveal a potential intermediate of the recognition process. The tRNA is positioned on the enzyme such that it cannot be aminoacylated but adopts an overall conformation similar to that observed in active complexes. While the anticodon loop binds to the N-terminal domain of the enzyme in a manner similar to that of the related active complexes, its aminoacyl acceptor arm remains at the entrance of the active site, stabilized in its intermediate conformational state by non-specific interactions with the insertion and catalytic domains. The thermophilic nature of the enzyme, which manifests itself in a very low kinetic efficiency at 17 degrees C, the temperature at which the crystals were grown, is in agreement with the relative stability of this non-productive conformational state. Based on these data, a pathway for tRNA binding and recognition is proposed.

About this Structure

1EFW is a Protein complex structure of sequences from Escherichia coli and Thermus thermophilus. Full crystallographic information is available from OCA.

Reference

An intermediate step in the recognition of tRNA(Asp) by aspartyl-tRNA synthetase., Briand C, Poterszman A, Eiler S, Webster G, Thierry J, Moras D, J Mol Biol. 2000 Jun 16;299(4):1051-60. PMID:10843857 Page seeded by OCA on Fri May 2 15:02:52 2008

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