Source:http://linkedlifedata.com/resource/pubmed/id/19656186
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
17
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pubmed:dateCreated |
2009-8-21
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pubmed:databankReference | |
pubmed:abstractText |
The ATP-pyrophosphate exchange reaction catalyzed by Arg-tRNA, Gln-tRNA and Glu-tRNA synthetases requires the assistance of the cognate tRNA. tRNA also assists Arg-tRNA synthetase in catalyzing the pyrophosphorolysis of synthetic Arg-AMP at low pH. The mechanism by which the 3'-end A76, and in particular its hydroxyl group, of the cognate tRNA is involved with the exchange reaction catalyzed by those enzymes has yet to be established. We determined a crystal structure of a complex of Arg-tRNA synthetase from Pyrococcus horikoshii, tRNA(Arg)(CCU) and an ATP analog with Rfactor = 0.213 (Rfree = 0.253) at 2.0 A resolution. On the basis of newly obtained structural information about the position of ATP bound on the enzyme, we constructed a structural model for a mechanism in which the formation of a hydrogen bond between the 2'-OH group of A76 of tRNA and the carboxyl group of Arg induces both formation of Arg-AMP (Arg + ATP --> Arg-AMP + pyrophosphate) and pyrophosphorolysis of Arg-AMP (Arg-AMP + pyrophosphate --> Arg + ATP) at low pH. Furthermore, we obtained a structural model of the molecular mechanism for the Arg-tRNA synthetase-catalyzed deacylation of Arg-tRNA (Arg-tRNA + AMP --> Arg-AMP + tRNA at high pH), in which the deacylation of aminoacyl-tRNA bound on Arg-tRNA synthetase and Glu-tRNA synthetase is catalyzed by a quite similar mechanism, whereby the proton-donating group (-NH-C+(NH2)2 or -COOH) of Arg and Glu assists the aminoacyl transfer from the 2'-OH group of tRNA to the phosphate group of AMP at high pH.
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pubmed:commentsCorrections | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adenylyl Imidodiphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Arginine,
http://linkedlifedata.com/resource/pubmed/chemical/Arginine-tRNA Ligase,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoric Acid Esters,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Transfer, Amino Acyl,
http://linkedlifedata.com/resource/pubmed/chemical/tRNA, arginine-
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
1742-4658
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pubmed:author | |
pubmed:issnType |
Electronic
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pubmed:volume |
276
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
4763-79
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pubmed:dateRevised |
2010-2-12
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pubmed:meshHeading |
pubmed-meshheading:19656186-Adenylyl Imidodiphosphate,
pubmed-meshheading:19656186-Amino Acid Sequence,
pubmed-meshheading:19656186-Arginine,
pubmed-meshheading:19656186-Arginine-tRNA Ligase,
pubmed-meshheading:19656186-Binding Sites,
pubmed-meshheading:19656186-Crystallography, X-Ray,
pubmed-meshheading:19656186-Hydrogen Bonding,
pubmed-meshheading:19656186-Models, Molecular,
pubmed-meshheading:19656186-Molecular Sequence Data,
pubmed-meshheading:19656186-Phosphoric Acid Esters,
pubmed-meshheading:19656186-Protein Binding,
pubmed-meshheading:19656186-Pyrococcus horikoshii,
pubmed-meshheading:19656186-RNA, Transfer, Amino Acyl,
pubmed-meshheading:19656186-Saccharomyces cerevisiae,
pubmed-meshheading:19656186-Thermus thermophilus
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pubmed:year |
2009
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pubmed:articleTitle |
Modeling of tRNA-assisted mechanism of Arg activation based on a structure of Arg-tRNA synthetase, tRNA, and an ATP analog (ANP).
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pubmed:affiliation |
Department of Chemistry and Biochemistry, Graduate School of Humanities and Sciences, Ochanomizu University, Tokyo, Japan. konno.michiko@ocha.ac.jp
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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