› 4hvk

X-ray diffraction
1.43Å resolution

Crystal structure and functional studies of an unusual L-cysteine desulfurase from Archaeoglobus fulgidus.

Released:
DOI: 10.2210/pdb4hvk/pdb
PDB entry 4hvk coloured by chain, front view.
PDB entry 4hvk coloured by chain, side view.
PDB entry 4hvk coloured by chain, top view.
Source organism: Archaeoglobus fulgidus DSM 4304
Primary publication:
Crystal structure and functional studies of an unusual L-cysteine desulfurase from Archaeoglobus fulgidus.
Yamanaka Y, Zeppieri L, Nicolet Y, Marinoni EN, de Oliveira JS, Odaka M, Dean DR, Fontecilla-Camps JC
Dalton Trans 42 3092-9 (2013)
PMID: 23160436

Function and Biology Details

Reaction catalysed: 
(1a) L-cysteine + [enzyme]-cysteine = L-alanine + [enzyme]-S-sulfanylcysteine
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-128158 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cysteine desulfurase IscS 2 Chain: A
Molecule details ›
Chain: A
Length: 382 amino acids
Theoretical weight: 41.89 KDa
Source organism: Archaeoglobus fulgidus DSM 4304
Expression system: Escherichia coli
UniProt:
  • Canonical: O29689 (Residues: 1-382; Coverage: 100%)
Gene names: AF_0564, iscS2
Sequence domains: Aminotransferase class-V
Structure domains:

Ligands and Environments


Cofactor: Ligand PMP 1 x PMP
3 bound ligands:
Ligand CA 2 x CA
Ligand CL 1 x CL
Ligand PG4 10 x PG4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: C2221
Unit cell:
a: 70.06Å b: 99.27Å c: 108.86Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.11 0.108 0.151
Expression system: Escherichia coli

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Citations

1 review citation

The role of FeS clusters for molybdenum cofactor biosynthesis and molybdoenzymes in bacteria.
Yokoyama et al. (2015)
6 other articles

2 mentions without citation

X-ray structures of Nfs2, the plastidial cysteine desulfurase from Arabidopsis thaliana.
Roret et al. (2014)
1 more