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

Vicky Tzu Jung Juan; Patrick Bajan; Chatchakorn Eurtivong; Tianyang Liu; Christopher J. Squire; Evelyn Yu Wen Huang; Ivanhoe K.H. Leung

doi:10.1039/d5cc05573c

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

Vicky Tzu Jung Juan
, Patrick Bajan
, Chatchakorn Eurtivong
, Tianyang Liu
, Christopher J. Squire
, Evelyn Yu Wen Huang
, Ivanhoe K.H. Leung

Department of Pharmaceutical Chemistry

University of Auckland
Bio21 Molecular Science and Biotechnology Institute
School of Biological Sciences

Research output: Contribution to journal › Article › peer-review

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.

Original language	English
Pages (from-to)	19020-19023
Number of pages	4
Journal	Chemical Communications
Volume	61
Issue number	96
DOIs	https://doi.org/10.1039/d5cc05573c
Publication status	Published - 24 Oct 2025

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

SDG 3 Good Health and Well-being

Access to Document

10.1039/d5cc05573c

Cite this

@article{5a0b46c53a794dfda2f639d409152482,

title = "Structural remodelling of the 2OG oxygenase Rv3406 enables sulfur-scavenging in Mycobacterium tuberculosis",

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.",

author = "Juan, \{Vicky Tzu Jung\} and Patrick Bajan and Chatchakorn Eurtivong and Tianyang Liu and Squire, \{Christopher J.\} and Huang, \{Evelyn Yu Wen\} and Leung, \{Ivanhoe K.H.\}",

note = "Publisher Copyright: This journal is {\textcopyright} The Royal Society of Chemistry, 2025",

year = "2025",

month = oct,

day = "24",

doi = "10.1039/d5cc05573c",

language = "English",

volume = "61",

pages = "19020--19023",

journal = "Chemical Communications",

issn = "1359-7345",

publisher = "Royal Society of Chemistry",

number = "96",

}

TY - JOUR

T1 - Structural remodelling of the 2OG oxygenase Rv3406 enables sulfur-scavenging in Mycobacterium tuberculosis

AU - Juan, Vicky Tzu Jung

AU - Bajan, Patrick

AU - Eurtivong, Chatchakorn

AU - Liu, Tianyang

AU - Squire, Christopher J.

AU - Huang, Evelyn Yu Wen

AU - Leung, Ivanhoe K.H.

PY - 2025/10/24

Y1 - 2025/10/24

N2 - 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.

AB - 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.

UR - https://www.scopus.com/pages/publications/105023196759

U2 - 10.1039/d5cc05573c

DO - 10.1039/d5cc05573c

M3 - Article

C2 - 41178574

AN - SCOPUS:105023196759

SN - 1359-7345

VL - 61

SP - 19020

EP - 19023

JO - Chemical Communications

JF - Chemical Communications

IS - 96

ER -

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

Abstract

UN SDGs

Access to Document

Other files and links

Fingerprint

Cite this