Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/145102
Title: Substrate-induced structural alterations of Mycobacterial mycothione reductase and critical residues involved
Authors: Kumar, Arvind
Subramanian Manimekalai, Malathy Sony
Grüber, Gerhard
Keywords: Science::Biological sciences
Issue Date: 2018
Source: Kumar, A., Subramanian Manimekalai, M. S., & Grüber, G. (2018). Substrate-induced structural alterations of Mycobacterial mycothione reductase and critical residues involved. FEBS Letters, 592(4), 568-585. doi:10.1002/1873-3468.12984
Journal: FEBS Letters
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.
URI: https://hdl.handle.net/10356/145102
ISSN: 1873-3468
DOI: 10.1002/1873-3468.12984
Schools: School of Biological Sciences 
Rights: © 2018 Federation of European Biochemical Societies (FEBS). All rights reserved.
Fulltext Permission: none
Fulltext Availability: No Fulltext
Appears in Collections:SBS Journal Articles

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