Structural remodelling of the 2OG oxygenase Rv3406 enables sulfur-scavenging in Mycobacterium tuberculosis

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dc.contributor.authorJuan V.T.J.
dc.contributor.authorBajan P.
dc.contributor.authorEurtivong C.
dc.contributor.authorLiu T.
dc.contributor.authorSquire C.J.
dc.contributor.authorHuang E.Y.W.
dc.contributor.authorLeung I.K.H.
dc.contributor.correspondenceJuan V.T.J.
dc.contributor.otherMahidol University
dc.date.accessioned2025-12-08T18:15:40Z
dc.date.available2025-12-08T18:15:40Z
dc.date.issued2025-10-24
dc.description.abstractRv3406 evolved from the ubiquitous taurine-catabolising enzyme TauD and functions as a sulfur-scavenging protein in Mycobacterium tuberculosis. Structural and biochemical analyses reveal specific changes that shape its chemical environment for ligand interaction and explain its broad substrate range. These findings show how amino acid substitutions redefine protein function and drive adaptation to the unique metabolic context of Mycobacteria.
dc.identifier.citationChemical Communications Vol.61 No.96 (2025) , 19020-19023
dc.identifier.doi10.1039/d5cc05573c
dc.identifier.eissn1364548X
dc.identifier.issn13597345
dc.identifier.pmid41178574
dc.identifier.scopus2-s2.0-105023196759
dc.identifier.urihttps://repository.li.mahidol.ac.th/handle/123456789/113438
dc.rights.holderSCOPUS
dc.subjectMaterials Science
dc.subjectChemical Engineering
dc.subjectChemistry
dc.titleStructural remodelling of the 2OG oxygenase Rv3406 enables sulfur-scavenging in Mycobacterium tuberculosis
dc.typeArticle
mu.datasource.scopushttps://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=105023196759&origin=inward
oaire.citation.endPage19023
oaire.citation.issue96
oaire.citation.startPage19020
oaire.citation.titleChemical Communications
oaire.citation.volume61
oairecerif.author.affiliationThe University of Auckland
oairecerif.author.affiliationMahidol University
oairecerif.author.affiliationSchool of Biological Sciences
oairecerif.author.affiliationBio21 Molecular Science and Biotechnology Institute

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