<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>7(1)</volume><submitter>Wong CF</submitter><pubmed_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 divergen</pubmed_abstract><journal>Scientific reports</journal><pagination>5159</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC5505994</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>AhpC of the mycobacterial antioxidant defense system and its interaction with its reducing partner Thioredoxin-C.</pubmed_title><pmcid>PMC5505994</pmcid><pubmed_authors>Wong CF</pubmed_authors><pubmed_authors>Saw WG</pubmed_authors><pubmed_authors>Bhushan S</pubmed_authors><pubmed_authors>Ragunathan P</pubmed_authors><pubmed_authors>Shin J</pubmed_authors><pubmed_authors>Gruber G</pubmed_authors><pubmed_authors>Subramanian Manimekalai MS</pubmed_authors><pubmed_authors>Kumar A</pubmed_authors><pubmed_authors>Yin Z</pubmed_authors></additional><is_claimable>false</is_claimable><name>AhpC of the mycobacterial antioxidant defense system and its interaction with its reducing partner Thioredoxin-C.</name><description>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 divergen</description><dates><release>2017-01-01T00:00:00Z</release><publication>2017 Jul</publication><modification>2026-05-05T11:08:31.848Z</modification><creation>2025-06-01T00:37:08.114Z</creation></dates><accession>S-EPMC5505994</accession><cross_references><pubmed>28698569</pubmed><doi>10.1038/s41598-017-05354-5</doi></cross_references></HashMap>