5C04
Crystal structure of the F37H mutant AhpE from Mycobacterium tuberculosis
Summary for 5C04
| Entry DOI | 10.2210/pdb5c04/pdb |
| Related | 1XVW 1XXU 4X0X 4X1U 4XIH |
| Descriptor | Putative peroxiredoxin MT2298 (2 entities in total) |
| Functional Keywords | oxidoreductase, 1-cys peroxiredoxin, peroxiredoxin, thioredoxin fold, mycobacterium tuberculosis, active site mutant |
| Biological source | Mycobacterium tuberculosis |
| Total number of polymer chains | 2 |
| Total formula weight | 33681.84 |
| Authors | Pallo, A.,Dufe, V.T.,Messens, J. (deposition date: 2015-06-12, release date: 2016-07-27, 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 Cited by 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: 27471753DOI: 10.1039/c6cc02645a PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.45 Å) |
Structure validation
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