Structural remodelling of the 2OG oxygenase Rv3406 enables sulfur-scavenging in Mycobacterium tuberculosis
1
Issued Date
2025-10-24
Resource Type
ISSN
13597345
eISSN
1364548X
Scopus ID
2-s2.0-105023196759
Pubmed ID
41178574
Journal Title
Chemical Communications
Volume
61
Issue
96
Start Page
19020
End Page
19023
Rights Holder(s)
SCOPUS
Bibliographic Citation
Chemical Communications Vol.61 No.96 (2025) , 19020-19023
Suggested Citation
Juan V.T.J., Bajan P., Eurtivong C., Liu T., Squire C.J., Huang E.Y.W., Leung I.K.H. Structural remodelling of the 2OG oxygenase Rv3406 enables sulfur-scavenging in Mycobacterium tuberculosis. Chemical Communications Vol.61 No.96 (2025) , 19020-19023. 19023. doi:10.1039/d5cc05573c Retrieved from: https://repository.li.mahidol.ac.th/handle/123456789/113438
Title
Structural remodelling of the 2OG oxygenase Rv3406 enables sulfur-scavenging in Mycobacterium tuberculosis
Corresponding Author(s)
Other Contributor(s)
Abstract
Rv3406 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.