Structural and functional consequences of mutating a proteobacteria-specific surface residue in the catalytic domain of Escherichia coli GluRS
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/j.febslet.2012.05.006/fullpdf
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4. Interactions between tRNA identity nucleotides and their recognition sites in glutaminyl-tRNA synthetase determine the cognate amino acid affinity of the enzyme;Ibba;Proc. Natl. Acad. Sci. USA,1996
5. Indirect readout of tRNA for aminoacylation;Perona;Biochemistry,2007
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3. Dispensability of zinc and the putative zinc-binding domain in bacterial glutamyl-tRNA synthetase;Bioscience Reports;2015-03-31
4. Preliminary X-ray crystallographic analysis of an engineered glutamyl-tRNA synthetase fromEscherichia coli;Acta Crystallographica Section F Structural Biology Communications;2014-06-18
5. Evolutionary insights about bacterial GlxRS from whole genome analyses: is GluRS2 a chimera?;BMC Evolutionary Biology;2014
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