Structural remodelling of the 2OG oxygenase Rv3406 enables sulfur-scavenging in <i>Mycobacterium tuberculosis</i>
Rv3406 evolved from the ubiquitous taurine-catabolising enzyme TauD and functions as a sulfur-scavenging protein in <i>Mycobacterium tuberculosis</i>. 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.
Authors
- Chatchakorn Eurtivong (ORCID: https://orcid.org/0000-0002-4501-5113)
- Ivanhoe K. H. Leung (ORCID: https://orcid.org/0000-0003-0633-6771)
- C.J. Squire (ORCID: https://orcid.org/0000-0001-9212-0461)
- Evelyn Yu‐Wen Huang (ORCID: https://orcid.org/0000-0002-3071-9759)
- Tianyang Liu
- Vicky Tzu-Jung Juan (ORCID: https://orcid.org/0000-0002-9208-2247)
- Patrick Bajan
Institutions
- University of Auckland (NZ)
- The University of Melbourne (AU)
- Mahidol University (TH)
- Maurice Wilkins Centre (NZ)
Publication Details
- Journal
- Chemical Communications
- Published
- 2025-01-01
- DOI
- https://doi.org/10.1039/d5cc05573c
- Primary Topic
- Chemical Reactions and Isotopes
- Type
- article
- Field-Weighted Citation Impact
- 0.00