1c0a
From Proteopedia
(New page: 200px<br /><applet load="1c0a" size="450" color="white" frame="true" align="right" spinBox="true" caption="1c0a, resolution 2.40Å" /> '''CRYSTAL STRUCTURE OF...) |
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| - | [[Image:1c0a.gif|left|200px]]<br /><applet load="1c0a" size=" | + | [[Image:1c0a.gif|left|200px]]<br /><applet load="1c0a" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1c0a, resolution 2.40Å" /> | caption="1c0a, resolution 2.40Å" /> | ||
'''CRYSTAL STRUCTURE OF THE E. COLI ASPARTYL-TRNA SYNTHETASE : TRNAASP : ASPARTYL-ADENYLATE COMPLEX'''<br /> | '''CRYSTAL STRUCTURE OF THE E. COLI ASPARTYL-TRNA SYNTHETASE : TRNAASP : ASPARTYL-ADENYLATE COMPLEX'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The 2.4 A crystal structure of the Escherichia coli aspartyl-tRNA | + | 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 Structure== | ==About this Structure== | ||
| - | 1C0A is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with SO4, AMP and AMO as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http:// | + | 1C0A is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=AMP:'>AMP</scene> and <scene name='pdbligand=AMO:'>AMO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C0A OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Dock-Bregeon, A | + | [[Category: Dock-Bregeon, A C.]] |
[[Category: Eiler, S.]] | [[Category: Eiler, S.]] | ||
[[Category: Moras, D.]] | [[Category: Moras, D.]] | ||
[[Category: Moulinier, L.]] | [[Category: Moulinier, L.]] | ||
| - | [[Category: Thierry, J | + | [[Category: Thierry, J C.]] |
[[Category: AMO]] | [[Category: AMO]] | ||
[[Category: AMP]] | [[Category: AMP]] | ||
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[[Category: protein-rna complex]] | [[Category: protein-rna complex]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:01:07 2008'' |
Revision as of 10:01, 21 February 2008
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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.
About this Structure
1C0A is a Protein complex structure of sequences from Escherichia coli with , and as ligands. Active as Aspartate--tRNA ligase, with EC number 6.1.1.12 Full crystallographic information is available from OCA.
Reference
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
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