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A promising strategy to combat TB is based on disrupting the mycobacterial redox homeostasis by inhibiting an NADPH\u2010dependent oxidoreductase, mycothione reductase (Mtr). Using high\u2010throughput screening, we recently identified potent and selective Mtr inhibitors. Here we report high\u2010resolution X\u2010ray structures of Mtr from\n                    <jats:italic>Mycobacterium tuberculosis<\/jats:italic>\n                    and\n                    <jats:italic>Mycobacterium xenopi,<\/jats:italic>\n                    including the\n                    <jats:italic>M. tuberculosis<\/jats:italic>\n                    enzyme complexed with a novel inhibitor, Respiri\u20101093. Our findings demonstrate that Respiri\u20101093 competes with the NADP(H) binding rather than mycothione binding. Analysis of the binding site explains the observed selectivity of the inhibitor towards the\n                    <jats:italic>M. tuberculosis<\/jats:italic>\n                    enzyme. These results provide a structural basis for rational drug design.\n                  <\/jats:p>","DOI":"10.1002\/1873-3468.70336","type":"journal-article","created":{"date-parts":[[2026,5,23]],"date-time":"2026-05-23T10:40:16Z","timestamp":1779532816000},"page":"2143-2153","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Crystal structure of\n                    <i>Mycobacterium tuberculosis<\/i>\n                    mycothione reductase in complex with a specific inhibitor reveals competition with\n                    <scp>NADP<\/scp>\n                    (H) binding"],"prefix":"10.1002","volume":"600","author":[{"given":"Lauren","family":"Oorts","sequence":"first","affiliation":[{"name":"Laboratory of Microbiology, Parasitology and Hygiene, Faculty of Pharmaceutical, Biomedical and Veterinary Sciences University of Antwerp  Wilrijk Belgium"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Evgenii 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