Correlations between kinetic and X-ray analyses of engineered enzymes: Crystal structures of mutants Cys arrow right Gly-35 and Tyr arrow right Phe-34 of tyrosyl-tRNA synthetase

The crystal structures of two mutant tyrosyl-tRNA synthetases (TyrTS) are reported to test predictions from kinetic data about structural perturbations and also to aid in the interpretation of apparent strengths of hydrogen bonds measured by protein engineering. The enzyme-tyrosine and enzyme-tyrosy...

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Published inBiochemistry (Easton) Vol. 30; no. 21; pp. 5157 - 5164
Main Authors Fothergill, MD, Fersht, A R
Format Journal Article
LanguageEnglish
Published 01.01.1991
Subjects
cysteine
tyrosine
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Summary:The crystal structures of two mutant tyrosyl-tRNA synthetases (TyrTS) are reported to test predictions from kinetic data about structural perturbations and also to aid in the interpretation of apparent strengths of hydrogen bonds measured by protein engineering. The enzyme-tyrosine and enzyme-tyrosyl adenylate complexes of the mutant, TyrTS(Cys arrow right Gly-35), have been determined at 2.5- and 2.7-Angstroms resolution, respectively.
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ISSN:0006-2960