Escherichia coli ilvN interacts with the FAD binding domain of ilvB and activates the AHAS I enzyme.

Abstract

The unique multidomain organization in the multimeric Escherichia coli AHAS I (ilvBN) enzyme has been exploited to generate polypeptide fragments which, when cloned and expressed, reassemble in the presence of cofactors to yield a catalytically competent enzyme. Multidimensional multinuclear NMR methods have been employed for obtaining near complete… (More)
DOI: 10.1021/bi701893b

10 Figures and Tables

Topics

  • Presentations referencing similar topics