1c0a: Difference between revisions
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[[Image:1c0a.gif|left|200px]] | [[Image:1c0a.gif|left|200px]] | ||
'''CRYSTAL STRUCTURE OF THE E. COLI ASPARTYL-TRNA SYNTHETASE : TRNAASP : ASPARTYL-ADENYLATE COMPLEX''' | {{Structure | ||
|PDB= 1c0a |SIZE=350|CAPTION= <scene name='initialview01'>1c0a</scene>, resolution 2.40Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene> and <scene name='pdbligand=AMO:ASPARTYL-ADENOSINE-5'-MONOPHOSPHATE'>AMO</scene> | |||
|ACTIVITY= [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] | |||
|GENE= | |||
}} | |||
'''CRYSTAL STRUCTURE OF THE E. COLI ASPARTYL-TRNA SYNTHETASE : TRNAASP : ASPARTYL-ADENYLATE COMPLEX''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1C0A is a [ | 1C0A is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C0A OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10562565 10562565] | ||
[[Category: Aspartate--tRNA ligase]] | [[Category: Aspartate--tRNA ligase]] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
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[[Category: protein-rna complex]] | [[Category: protein-rna complex]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:18:16 2008'' | ||
Revision as of 11:18, 20 March 2008
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| , resolution 2.40Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , and | ||||||
| Activity: | Aspartate--tRNA ligase, with EC number 6.1.1.12 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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