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› 6uy5

X-ray diffraction
1.5Å resolution

E. coli cysteine desulfurase SufS with a spontaneously rotated beta-hairpin

Released:
DOI: 10.2210/pdb6uy5/pdb
Model geometry
Fit model/data
PDB entry 6uy5 coloured by chain, front view.
PDB entry 6uy5 coloured by chain, side view.
PDB entry 6uy5 coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
Structural evidence for a latch mechanism regulating access to the active site of SufS-family cysteine desulfurases
Dunkle JA, Bruno MR, Frantom PA
Acta Crystallogr. D Biol. Crystallogr. 76 291-301 (2020)

Function and Biology Details

Reactions catalysed: 
(sulfur carrier)-H + L-cysteine = (sulfur carrier)-SH + L-alanine.
L-selenocysteine + AH2 = hydrogenselenide + L-alanine + A + H(+).
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-160167 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cysteine desulfurase Chains: A, B
Molecule details ›
Chains: A, B
Length: 406 amino acids
Theoretical weight: 44.51 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P77444 (Residues: 1-406; Coverage: 100%)
Gene names: JW1670, b1680, csdB, sufS, ynhB
Sequence domains: Aminotransferase class-V

Ligands and Environments


Cofactor: Ligand PLP 2 x PLP
No bound ligands
1 modified residue:
Ligand CSS 2 x CSS

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P21
Unit cell:
a: 60.54Å b: 115.74Å c: 63.66Å
α: 90° β: 114.47° γ: 90°
R-values:
R R work R free
0.197 0.197 0.221
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 citation in other articles

Structural and Biochemical Characterization of Mycobacterium tuberculosis Zinc SufU-SufS Complex.
Elchennawi et al. (2023)
1 more

3 mentions without citation

The Multifaceted Bacterial Cysteine Desulfurases: From Metabolism to Pathogenesis.
Das et al. (2021)
2 more