The covalent complex of Jo-In results from a long-lived, non-covalent intermediate state with near-native structure - Archive ouverte HAL Access content directly
Journal Articles Biochemical and Biophysical Research Communications Year : 2021

The covalent complex of Jo-In results from a long-lived, non-covalent intermediate state with near-native structure

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Neil Cox
Cyril Charlier
  • Function : Author
  • PersonId : 1109653
Marion de La Mare
  • Function : Author
  • PersonId : 976152
Sophie Barbe
Isabelle André
Guy Lippens
Cédric Montanier
  • Function : Author
  • PersonId : 1155910

Abstract

Covalent protein complexes have been used to assemble enzymes in large scaffolds for biotechnology purposes. Although the catalytic mechanism of the covalent linking of such proteins is well known, the recognition and overall structural mechanisms driving the association are far less understood but could help further functional engineering of these complexes. Here, we study the Jo-In complex by NMR spectroscopy and molecular modelling. We characterize a transient non-covalent complex, with structural elements close to those in the final covalent complex. Using site specific mutagenesis, we further show that this non-covalent association is essential for the covalent complex to form
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hal-03554277 , version 1 (24-10-2022)

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Neil Cox, Cyril Charlier, Ramadoss Vijayaraj, Marion de La Mare, Sophie Barbe, et al.. The covalent complex of Jo-In results from a long-lived, non-covalent intermediate state with near-native structure. Biochemical and Biophysical Research Communications, 2021, 589, pp.223-228. ⟨10.1016/j.bbrc.2021.12.028⟩. ⟨hal-03554277⟩
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