1c0a: Difference between revisions

Revision as of 12:10, 2 May 2008

CRYSTAL STRUCTURE OF THE E. COLI ASPARTYL-TRNA SYNTHETASE : TRNAASP : ASPARTYL-ADENYLATE COMPLEX

OverviewOverview

The 2.4 A crystal structure of the Escherichia coli aspartyl-tRNA synthetase (AspRS)-tRNA(Asp)-aspartyl-adenylate complex shows the two substrates poised for the transfer of the aspartic acid moiety from the adenylate to the 3'-hydroxyl of the terminal adenosine of the tRNA. A general molecular mechanism is proposed for the second step of the aspartylation reaction that accounts for the observed conformational changes, notably in the active site pocket. The stabilization of the transition state is mediated essentially by two amino acids: the class II invariant arginine of motif 2 and the eubacterial-specific Gln231, which in eukaryotes and archaea is replaced by a structurally non-homologous serine. Two archetypal RNA-protein modes of interactions are observed: the anticodon stem-loop, including the wobble base Q, binds to the N-terminal beta-barrel domain through direct protein-RNA interactions, while the binding of the acceptor stem involves both direct and water-mediated hydrogen bonds in an original recognition scheme.

About this StructureAbout this Structure

1C0A is a Protein complex structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

Synthesis of aspartyl-tRNA(Asp) in Escherichia coli--a snapshot of the second step., Eiler S, Dock-Bregeon A, Moulinier L, Thierry JC, Moras D, EMBO J. 1999 Nov 15;18(22):6532-41. PMID:10562565 Page seeded by OCA on Fri May 2 12:10:57 2008

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OCA

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 [[Image:1c0a.gif|left|200px]]
- {{Structure
+<!--
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+The line below this paragraph, containing "STRUCTURE_1c0a", creates the "Structure Box" on the page.
-|SITE=
+You may change the PDB parameter (which sets the PDB file loaded into the applet)
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+or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-|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>
+or leave the SCENE parameter empty for the default display.
-|GENE=
+-->
-|DOMAIN=
+{{STRUCTURE_1c0a|  PDB=1c0a  |  SCENE=  }}
-|RELATEDENTRY=
-|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1c0a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c0a OCA], [http://www.ebi.ac.uk/pdbsum/1c0a PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1c0a RCSB]</span>
-}}
 '''CRYSTAL STRUCTURE OF THE E. COLI ASPARTYL-TRNA SYNTHETASE : TRNAASP : ASPARTYL-ADENYLATE COMPLEX'''
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 [[Category: Moulinier, L.]]
 [[Category: Thierry, J C.]]
-[[Category: protein-rna complex]]
+[[Category: Protein-rna complex]]
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 12:10:57 2008''
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:11:57 2008''