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Sieves in sequence.

作者信息

Fersht A R

机构信息

Department of Chemistry and Centre for Protein Engineering, Cambridge CB2 1EW, UK.

出版信息

Science. 1998 Apr 24;280(5363):541. doi: 10.1126/science.280.5363.541.

DOI:10.1126/science.280.5363.541

PMID:9575099

Abstract

摘要

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Sieves in sequence.

Science. 1998 Apr 24;280(5363):541. doi: 10.1126/science.280.5363.541.

Enzyme structure with two catalytic sites for double-sieve selection of substrate.

Science. 1998 Apr 24;280(5363):578-82. doi: 10.1126/science.280.5363.578.

Crystal structures of the CP1 domain from Thermus thermophilus isoleucyl-tRNA synthetase and its complex with L-valine.

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Mutational isolation of a sieve for editing in a transfer RNA synthetase.

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Structural basis for substrate recognition by the editing domain of isoleucyl-tRNA synthetase.

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Isoleucyl-tRNA synthetase from Escherichia coli MRE 600: discrimination between isoleucine and valine with modulated accuracy.

Biol Chem Hoppe Seyler. 1987 Mar;368(3):229-37. doi: 10.1515/bchm3.1987.368.1.229.

[Superspecificity of aminoacyl-tRNA-synthases].

Mol Biol (Mosk). 1984 Jan-Feb;18(1):205-26.

Effect of inorganic pyrophosphate on the pretransfer proofreading in the isoleucyl-tRNA synthetase from Escherichia coli.

Eur J Biochem. 1992 Dec 1;210(2):451-4. doi: 10.1111/j.1432-1033.1992.tb17441.x.

Kinetic proofreading at single molecular level: aminoacylation of tRNA(Ile) and the role of water as an editor.

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Errors from selective disruption of the editing center in a tRNA synthetase.

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A glycine hinge for tRNA-dependent translocation of editing substrates to prevent errors by leucyl-tRNA synthetase.

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Sieves in sequence.

Science. 1998 Apr 24;280(5363):541. doi: 10.1126/science.280.5363.541.

Enzyme structure with two catalytic sites for double-sieve selection of substrate.

Science. 1998 Apr 24;280(5363):578-82. doi: 10.1126/science.280.5363.578.

Crystal structures of the CP1 domain from Thermus thermophilus isoleucyl-tRNA synthetase and its complex with L-valine.

J Biol Chem. 2004 Feb 27;279(9):8396-402. doi: 10.1074/jbc.M312830200. Epub 2003 Dec 12.

Mutational isolation of a sieve for editing in a transfer RNA synthetase.

Science. 1994 Apr 8;264(5156):265-7. doi: 10.1126/science.8146659.

Structural basis for substrate recognition by the editing domain of isoleucyl-tRNA synthetase.

J Mol Biol. 2006 Jun 16;359(4):901-12. doi: 10.1016/j.jmb.2006.04.025. Epub 2006 Apr 25.

Isoleucyl-tRNA synthetase from Escherichia coli MRE 600: discrimination between isoleucine and valine with modulated accuracy.

Biol Chem Hoppe Seyler. 1987 Mar;368(3):229-37. doi: 10.1515/bchm3.1987.368.1.229.

[Superspecificity of aminoacyl-tRNA-synthases].

Mol Biol (Mosk). 1984 Jan-Feb;18(1):205-26.

Effect of inorganic pyrophosphate on the pretransfer proofreading in the isoleucyl-tRNA synthetase from Escherichia coli.

Eur J Biochem. 1992 Dec 1;210(2):451-4. doi: 10.1111/j.1432-1033.1992.tb17441.x.

Kinetic proofreading at single molecular level: aminoacylation of tRNA(Ile) and the role of water as an editor.

PLoS One. 2013 Jun 20;8(6):e66112. doi: 10.1371/journal.pone.0066112. Print 2013.

Errors from selective disruption of the editing center in a tRNA synthetase.

Biochemistry. 2000 Jul 18;39(28):8180-6. doi: 10.1021/bi0004798.

Coordination of tRNA synthetase active sites for chemical fidelity.

J Biol Chem. 2012 Mar 30;287(14):11285-9. doi: 10.1074/jbc.C111.325795. Epub 2012 Feb 13.

Substrate specificity of bacterial prolyl-tRNA synthetase editing domain is controlled by a tunable hydrophobic pocket.

J Biol Chem. 2012 Jan 27;287(5):3175-84. doi: 10.1074/jbc.M111.313619. Epub 2011 Nov 29.

Naturally occurring aminoacyl-tRNA synthetases editing-domain mutations that cause mistranslation in Mycoplasma parasites.

Proc Natl Acad Sci U S A. 2011 Jun 7;108(23):9378-83. doi: 10.1073/pnas.1016460108. Epub 2011 May 23.

Mechanistic insights into cognate substrate discrimination during proofreading in translation.

Proc Natl Acad Sci U S A. 2010 Dec 21;107(51):22117-21. doi: 10.1073/pnas.1014299107. Epub 2010 Nov 22.

Paradox of mistranslation of serine for alanine caused by AlaRS recognition dilemma.

Nature. 2009 Dec 10;462(7274):808-12. doi: 10.1038/nature08612.

Revisiting the operational RNA code for amino acids: Ensemble attributes and their implications.

RNA. 2010 Jan;16(1):141-53. doi: 10.1261/rna.1745910. Epub 2009 Dec 1.

A glycine hinge for tRNA-dependent translocation of editing substrates to prevent errors by leucyl-tRNA synthetase.

FEBS Lett. 2009 Nov 3;583(21):3443-7. doi: 10.1016/j.febslet.2009.09.039. Epub 2009 Sep 29.

Defects in transient tRNA translocation bypass tRNA synthetase quality control mechanisms.

J Biol Chem. 2009 Apr 24;284(17):11478-84. doi: 10.1074/jbc.M807395200. Epub 2009 Mar 3.

Sieves in sequence.

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