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

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

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

http://www.wikidata.org/entity/Q35728198

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Elongation Factor Tu Prevents Misediting of Gly-tRNA(Gly) Caused by the Design Behind the Chiral Proofreading Site of D-Aminoacyl-tRNA Deacylase Essentiality Assessment of Cysteinyl and Lysyl-tRNA Synthetases of Mycobacterium smegmatis Specificity and catalysis hardwired at the RNA-protein interface in a translational proofreading enzyme.Kinetic partitioning between synthetic and editing pathways in class I aminoacyl-tRNA synthetases occurs at both pre-transfer and post-transfer hydrolytic steps Aminoacyl-tRNA substrate and enzyme backbone atoms contribute to translational quality control by YbaK Exclusive use of trans-editing domains prevents proline mistranslation A multiple aminoacyl-tRNA synthetase complex that enhances tRNA-aminoacylation in African trypanosomes.Strictly conserved lysine of prolyl-tRNA Synthetase editing domain facilitates binding and positioning of misacylated tRNA(Pro.).Substrate and enzyme functional groups contribute to translational quality control by bacterial prolyl-tRNA synthetase.Conformational and chemical selection by a trans-acting editing domain.Quality control by trans-editing factor prevents global mistranslation of non-protein amino acid α-aminobutyrate.

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P2860

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

http://www.wikidata.org/entity/Q35728198

description

2011 nî lūn-bûn

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Substrate specificity of bacte ...... y a tunable hydrophobic pocket

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Substrate specificity of bacte ...... y a tunable hydrophobic pocket

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JBC.M111.313619

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Journal of Biological Chemistry

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Substrate specificity of bacte ...... y a tunable hydrophobic pocket

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Christopher M Hadad

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Mom Das

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Sandeep Kumar

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P2860

Post-transfer editing in vitro and in vivo by the beta subunit of phenylalanyl-tRNA synthetase

A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

Comparison of simple potential functions for simulating liquid water

Crystal structure of YbaK protein from Haemophilus influenzae (HI1434) at 1.8 A resolution: functional implications

Structural basis for double-sieve discrimination of L-valine from L-isoleucine and L-threonine by the complex of tRNA(Val) and valyl-tRNA synthetase

Transfer RNA-mediated editing in threonyl-tRNA synthetase. The class II solution to the double discrimination problem

The structure of alanyl-tRNA synthetase with editing domain

Trans-editing of mischarged tRNAs.

Editing-defective tRNA synthetase causes protein misfolding and neurodegeneration

A point-charge force field for molecular mechanics simulations of proteins based on condensed-phase quantum mechanical calculations

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3175-3184

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scholarly article

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5

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287

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Karin Musier-Forsyth

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22128149

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