Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/88317
Title: AhpC of the mycobacterial antioxidant defense system and its interaction with its reducing partner Thioredoxin-C
Authors: Wong, Chui Fann
Shin, Joon
Manimekalai, Malathy Sony Subramanian
Saw, Wuan Geok
Yin, Zhan
Bhushan, Shashi
Kumar, Arvind
Ragunathan, Priya
Grüber, Gerhard
Keywords: Thioredoxin and Peroxiredoxin System
AhpC
Issue Date: 2017
Source: Wong, C. F., Shin, J., Manimekalai, M. S. S., Saw, W. G., Yin, Z., Bhushan, S., et al. (2017). AhpC of the mycobacterial antioxidant defense system and its interaction with its reducing partner Thioredoxin-C. Scientific Reports, 7(1), 5159-.
Series/Report no.: Scientific Reports
Abstract: Despite the highly oxidative environment of the phagosomal lumen, the need for maintaining redox homeostasis is a critical aspect of mycobacterial biology. The pathogens are equipped with the sophisticated thioredoxin- (Trx) and peroxiredoxin system, including TrxC and the alkyl hydroperoxide reductase subunit C (AhpC), whereby TrxC is one of the reducing partners of AhpC. Here we visualize the redox modulated dodecamer ring formation of AhpC from Mycobacterium bovis (BCG strain; MbAhpC) using electron microscopy and present novel insights into the unique N-terminal epitope (40 residues) of mycobacterial AhpC. Truncations and amino acid substitutions of residues in the unique N-terminus of MbAhpC provide insights into their structural and enzymatic roles, and into the evolutionary divergence of mycobacterial AhpC versus that of other bacteria. These structural details shed light on the epitopes and residues of TrxC which contributes to its interaction with AhpC. Since human cells lack AhpC, the unique N-terminal epitope of mycobacterial AhpC as well as the MbAhpC-TrxC interface represent an ideal drug target.
URI: https://hdl.handle.net/10356/88317
http://hdl.handle.net/10220/44598
ISSN: 2045-2322
DOI: http://dx.doi.org/10.1038/s41598-017-05354-5
Rights: © 2017 The Author(s) (Nature Publishing Group). This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.
Fulltext Permission: open
Fulltext Availability: With Fulltext
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