Structural consequences of a one atom mutation on aspartate transcarbamylase from E. coli

FEBS Letters

Cherfils, J.³  Sweet, R.M.¹  Tauc, P.⁵  Middleton, S.A.²  Kantrowitz, E.R.²  Vachette, P.⁴ 

[1] Department of Biology, Center for Structural Biology, Brookhaven National Laboratory, Upton, LI 11973, France;Department of Chemistry, Boston College, Chestnut Hill, MA 02167, USA;Laboratoire de Biologie Physicochimique, Bât. 430, Université Paris-Sud, 91405 Orsay, France;LURE, Bât. 209d, Université Paris-Sud, 91405 Orsay, France;Laboratoire d'Enzymologie, CNRS, 91190 Gif-sur-Yvette, France

关键词: Aspartate transcarbamylase;    Single amino acid mutation;    X-ray solution scattering;    Energy minimization;    Computer graphics;    ATCase;    aspartate transcarbamylase (EC 2.1.3.2);    Tyr-240→Phe;    mutant enzyme;    PALA;    N-phosphonacetyl-L-aspartate;    rms;    root mean square;   

DOI  :  10.1016/0014-5793(89)81371-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown