Isolation and characterization of an Escherichia coli seryl-tRNA synthetase mutant with a large increase in Km for serine.

Abstract:

:A mutant of Escherichia coli resistant to serine hydroxamate which has a large increase in Km for serine of seryl-tRNA synthetase is described. The mutant serS gene was cloned and sequenced and was found to contain a single-base-pair mutation, resulting in the substitution of the residue alanine 262 by valine in motif 2. The methyl side chain of alanine 262 is not exposed at the active site, and molecular modeling indicated that replacement of alanine 262 by valine does not significantly affect the configuration of amino acids at the active site. This finding suggests that the residue at this position may be involved in a conformational change (possibly induced by ATP binding) which is necessary for optimal binding of the cognate amino acid.

journal_name

J Bacteriol

journal_title

Journal of bacteriology

authors

Willison JC,Härtlein M,Leberman R

doi

10.1128/jb.177.11.3347-3350.1995

subject

Has Abstract

pub_date

1995-06-01 00:00:00

pages

3347-50

issue

11

eissn

0021-9193

issn

1098-5530

journal_volume

177

pub_type

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