4XIH

Crystal structure of the R116A mutant AhpE from Mycobacterium tuberculosis

Summary for 4XIH

• Entry DOI: 10.2210/pdb4xih/pdb
• Related: 1XVW 1XXU 4X0X 4X1U
• Descriptor: AhpC/TSA family protein (2 entities in total)
• Functional Keywords: peroxiredoxins, oxidoreductase
• Biological source: Mycobacterium tuberculosis (strain CCDC5079)
• Total number of polymer chains: 2
• Total formula weight: 33629.80

Authors

Tamu Dufe, V.,van Molle, I.,Pallo, A.,Messens, J. (deposition date: 2015-01-07, release date: 2016-06-29, Last modification date: 2024-01-10)

Primary citation

Pedre, B.,van Bergen, L.A.,Pallo, A.,Rosado, L.A.,Dufe, V.T.,Molle, I.V.,Wahni, K.,Erdogan, H.,Alonso, M.,Proft, F.D.,Messens, J.
The active site architecture in peroxiredoxins: a case study on Mycobacterium tuberculosis AhpE.
Chem.Commun.(Camb.), 52:10293-10296, 2016

PubMed Abstract: Peroxiredoxins catalyze the reduction of peroxides, a process of vital importance to survive oxidative stress. A nucleophilic cysteine, also known as the peroxidatic cysteine, is responsible for this catalytic process. We used the Mycobacterium tuberculosis alkyl hydroperoxide reductase E (MtAhpE) as a model to investigate the effect of the chemical environment on the specificity of the reaction. Using an integrative structural (R116A - PDB ; F37H - PDB ), kinetic and computational approach, we explain the mutational effects of key residues in its environment. This study shows that the active site residues are specifically oriented to create an environment which selectively favours a reaction with peroxides.

PubMed: 27471753
DOI: 10.1039/c6cc02645a

Experimental method

X-RAY DIFFRACTION (2.25 Å)