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8EVN

Sulfatase from Mycobacterium tuberculosis (Rv3406) in complex with N-oxalylglycine (NOG)

Summary for 8EVN
Entry DOI10.2210/pdb8evn/pdb
Related4FFA
DescriptorAlpha-ketoglutarate-dependent sulfate ester dioxygenase, N-OXALYLGLYCINE, NICKEL (II) ION, ... (5 entities in total)
Functional Keywordsoxidoreductase-inhibitor complex, sulfatase, 2-oxoglutarate dependent dioxygenase, oxidoreductase/inhibitor
Biological sourceMycobacterium tuberculosis
Total number of polymer chains4
Total formula weight132549.81
Authors
Juan, T.-J.,Leung, I.,Squire, C.J. (deposition date: 2022-10-20, release date: 2023-10-25, Last modification date: 2026-03-18)
Primary citationJuan, V.T.,Bajan, P.,Eurtivong, C.,Liu, T.,Squire, C.J.,Huang, E.Y.,Leung, I.K.H.
Structural remodelling of the 2OG oxygenase Rv3406 enables sulfur-scavenging in Mycobacterium tuberculosis.
Chem.Commun.(Camb.), 61:19020-19023, 2025
Cited by
PubMed Abstract: Rv3406 evolved from the ubiquitous taurine-catabolising enzyme TauD and functions as a sulfur-scavenging protein in . 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.
PubMed: 41178574
DOI: 10.1039/d5cc05573c
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.644 Å)
Structure validation

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