ISDA: 8EVN

Deposition Date 2022-10-20

Release Date 2023-10-25

Last Version Date 2026-03-18

Entry Detail

PDB ID:

8EVN

Keywords:

OXIDOREDUCTASE/INHIBITOR

Title:

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

Biological Source:

Source Organism(s):

Mycobacterium tuberculosis (Taxon ID: 1773)

Expression System(s):

Escherichia coli

Method Details:

Experimental Method:

X-RAY DIFFRACTION

Resolution:

2.64 Å

R-Value Free:

0.29

R-Value Work:

0.25

Space Group:

P 21 21 21

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Macromolecular Entities

Structures with similar UniProt ID

Protein Blast

Polymer Type:polypeptide(L)
Molecule:Alpha-ketoglutarate-dependent
Gene (Uniprot):MTCY78.22c
Chain IDs:A, B, C, D
Chain Length:298
Number of Molecules:4
Biological Source:Mycobacterium tuberculosis

UniProt ID:P9WKZ1 Pfam ID:PF02668 EC:1.14.11.77

Ligand Molecules

OGA

TRS

Primary Citation

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

Juan, V.T, Bajan, P, Eurtivong, C, Liu, T, Squire, C.J, Huang, E.Y, Leung, I.K.H.Show

Chem. Commun. (Camb.) 61 19020 19023 (2025)

PMID: 41178574 DOI: 10.1039/d5cc05573c

Abstact

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.

Legend

Protein

Chemical

Disease

Primary Citation of related structures

Abstact

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