1c0a: Difference between revisions

Revision as of 20:02, 30 June 2008

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File:1c0a.png

Template:STRUCTURE 1c0a

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

Template:ABSTRACT PUBMED 10562565

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 Mon Jun 30 20:02:04 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''CRYSTAL STRUCTURE OF THE E. COLI ASPARTYL-TRNA SYNTHETASE : TRNAASP : ASPARTYL-ADENYLATE COMPLEX'''
+===CRYSTAL STRUCTURE OF THE E. COLI ASPARTYL-TRNA SYNTHETASE : TRNAASP : ASPARTYL-ADENYLATE COMPLEX===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_10562565}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_10562565}}
 ==About this Structure==
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 [[Category: Thierry, J C.]]
 [[Category: Protein-rna complex]]
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