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Structural consequences of a one atom mutation on aspartate transcarbamylase from E. coli
Author(s) -
Cherfils J.,
Sweet R.M.,
Middleton S.A.,
Kantrowitz E.R.,
Tauc P.,
Vachette P.
Publication year - 1989
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(89)81371-7
Subject(s) - mutation , escherichia coli , aspartate carbamoyltransferase , genetics , chemistry , biology , gene
Tyr‐240 of the catalytic chain of aspartate transcarbamylase from E. coli has been substituted by Phe using site‐directed mutagenesis. The regulatory mechanisms of the mutant enzyme have been shown to be slightly less effective than the wild‐type enzyme [1]. A study of the structural consequences of the mutation using solution X‐ray scattering and computer simulations is reported here. No significant change from the wild‐type enzyme is detectable in the quaternary structure. Simulations suggest that the only effect of the mutation is an increased mobility of the mutated side chain.