7BZ6

Mycobacterium bovis AhpC

Summary for 7BZ6

• Entry DOI: 10.2210/pdb7bz6/pdb
• Descriptor: Alkyl hydroperoxide reductase C peptide (1 entity in total)
• Functional Keywords: alkyl hydroperoxidase c, oxidoreductase
• Biological source: Mycobacterium bovis
• Total number of polymer chains: 2
• Total formula weight: 44886.02

Authors

Chong, S.M.S.,Neelagandan, K.,Gruber, G. (deposition date: 2020-04-27, release date: 2021-03-10, Last modification date: 2023-11-29)

Primary citation

Chong, S.M.S.,Kamariah, N.,Gruber, G.
Residues of helix alpha2 are critical for catalytic efficiency of mycobacterial alkylhydroperoxide reductase subunit C.
Febs Lett., 594:2829-2839, 2020

PubMed Abstract: The ability of Mycobacteria to overcome oxidative stress is of paramount importance for its survival within the host. One of the key enzymes that are involved in protecting the bacterium from reactive oxygen species is the catalase-peroxidase (KatG). However, in strains resistant to the antibiotic isoniazid, KatG is rendered ineffective, which is associated with an increased expression of alkylhydroperoxide reductase subunit C (AhpC). Mycobacterial AhpC possesses a unique helical displacement when compared to its bacterial counterparts. Here, via mutagenesis studies, we demonstrate the importance of this helix for redox modulation of the catalytic activity of AhpC. Along with structural insights from crystallographic data, the impact of critical residues on the structure and flexibility of the helix and on AhpC oligomerization is described.

PubMed: 32557576
DOI: 10.1002/1873-3468.13864

Experimental method

X-RAY DIFFRACTION (3.302 Å)