› 4isy

X-ray diffraction
2.59Å resolution

Crystal structure of IscS from Mycobacterium tuberculosis

Released:
DOI: 10.2210/pdb4isy/pdb
PDB entry 4isy coloured by chain, front view.
PDB entry 4isy coloured by chain, side view.
PDB entry 4isy coloured by chain, top view.
Source organism: Mycobacterium tuberculosis
Primary publication:
The cysteine desulfurase IscS of Mycobacterium tuberculosis is involved in iron-sulfur cluster biogenesis and oxidative stress defence.
Rybniker J, Pojer F, Marienhagen J, Kolly GS, Chen JM, van Gumpel E, Hartmann P, Cole ST
Biochem J 459 467-78 (2014)
PMID: 24548275

Function and Biology Details

Reaction catalysed: 
(1a) L-cysteine + [enzyme]-cysteine = L-alanine + [enzyme]-S-sulfanylcysteine
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-162050 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
IscS-like cysteine desulfurase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 404 amino acids
Theoretical weight: 42.5 KDa
Source organism: Mycobacterium tuberculosis
Expression system: Escherichia coli
UniProt:
  • Canonical: P9WQ71 (Residues: 2-393; Coverage: 100%)
Gene names: Rv3025c, iscS
Sequence domains: Aminotransferase class-V
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand GOL 8 x GOL
Ligand SO4 1 x SO4
1 modified residue:
Ligand LLP 4 x LLP

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06DA
Spacegroup: P1
Unit cell:
a: 66.814Å b: 78.131Å c: 92.774Å
α: 94.54° β: 104.71° γ: 98.57°
R-values:
R R work R free
0.189 0.186 0.245
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Chemistry and Redox Biology of Mycothiol.
Reyes et al. (2018)
3 more

1 mention without citation

Structural evidence for a latch mechanism regulating access to the active site of SufS-family cysteine desulfurases.
Dunkle et al. (2020)