Mécanisme et spécificité structurale des Méthionine sulfoxyde réductases (Msr) de Neisseria meningitidis et rôle du métal dans les MsrB

Abstract : Methionine sulfoxide reductases (Msr) allow cells to restore function of oxidized proteins on their methionine residues. In the first part, the catalytic mechanism of the MsrA and MsrB of the PilB protein from the bacterial pathogen Neisseria meningitidis has been studied. The two structurally unrelated classes of Msrs display a similar three step catalytic mechanism including the formation of a sulfenic acid intermediate followed by the formation of an intra disulfide bond which is reduced by thioredoxin (Trx). The two classes of Msrs conversely present an opposite stereoselectivity towards the sulfoxide function. In the second part, the three steps of the MsrBs catalytic mechanism have been kinetically characterized. The study of the role of the catalytic amino acid, the characterisation of the MsrB-Trx interaction and, the study of the role of the coordinated metal have also been investigated.
Document type :
Theses
Complete list of metadatas

https://hal.univ-lorraine.fr/tel-01754425
Contributor : Thèses Ul <>
Submitted on : Friday, March 30, 2018 - 9:48:47 AM
Last modification on : Monday, April 16, 2018 - 10:42:05 AM

File

SCD_T_2005_0004_OLRY.pdf
Files produced by the author(s)

Identifiers

  • HAL Id : tel-01754425, version 1

Collections

Citation

Alexandre Olry. Mécanisme et spécificité structurale des Méthionine sulfoxyde réductases (Msr) de Neisseria meningitidis et rôle du métal dans les MsrB. Sciences agricoles. Université Henri Poincaré - Nancy 1, 2005. Français. ⟨NNT : 2005NAN10004⟩. ⟨tel-01754425⟩

Share

Metrics

Record views

97

Files downloads

101