Abstract:
:Redox homeostasis is a prerequisite for survival of the pathogen Mycobacterium tuberculosis (Mtb) which employs the low molecular weight thiol mycothiol (MSH). The Mycobacterial NADPH-dependent mycothione reductase (MtMtr), composed of an NADPH-, FAD-, and a dimerization-domain connected by linkers, regulates the balance of oxidized-reduced MSH. Here, we demonstrate by small-angle X-ray scattering, that NADPH-binding alters the oligomeric state equilibrium of the protein with no significant overall structural change after MSH-binding. Mutation of critical residues in the linker regions of MtMtr eliminate partially or totally the NADPH-induced oligomerization effect with simultaneous effect on enzyme activity. The data provide insight into the MtMtr linker regions involved in the novel oligomerization equilibrium of the Mycobacterial enzyme.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Kumar A,Subramanian Manimekalai MS,Grüber Gdoi
10.1002/1873-3468.12984subject
Has Abstractpub_date
2018-02-01 00:00:00pages
568-585issue
4eissn
0014-5793issn
1873-3468journal_volume
592pub_type
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