› 4jyd

X-ray diffraction
1.71Å resolution

X-ray snapshots of possible intermediates in the time course of synthesis and degradation of protein-bound Fe4S4 clusters.

Released:
DOI: 10.2210/pdb4jyd/pdb
PDB entry 4jyd coloured by chain, front view.
PDB entry 4jyd coloured by chain, side view.
PDB entry 4jyd coloured by chain, top view.
Source organism: Thermotoga maritima MSB8
Primary publication:
X-ray snapshots of possible intermediates in the time course of synthesis and degradation of protein-bound Fe4S4 clusters.
Nicolet Y, Rohac R, Martin L, Fontecilla-Camps JC
Proc Natl Acad Sci U S A 110 7188-92 (2013)
PMID: 23596207

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-194758 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
[FeFe] hydrogenase maturase subunit HydE Chain: A
Molecule details ›
Chain: A
Length: 348 amino acids
Theoretical weight: 39.87 KDa
Source organism: Thermotoga maritima MSB8
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9X0Z6 (Residues: 1-348; Coverage: 100%)
Gene names: THEMA_07990, TM_1269, Tmari_1274
Sequence domains: Radical SAM superfamily
Structure domains: Aldolase class I

Ligands and Environments

7 bound ligands:
Ligand SF4 1 x SF4
Ligand SAH 1 x SAH
Ligand CPS 1 x CPS
Ligand 1N7 4 x 1N7
Ligand FE 1 x FE
Ligand H2S 2 x H2S
Ligand BR 4 x BR
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-2
Spacegroup: P212121
Unit cell:
a: 50.598Å b: 78.699Å c: 85.96Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.192 0.189 0.251
Expression system: Escherichia coli

Quick links

Citations

6 review citations

Metalloproteins containing cytochrome, iron-sulfur, or copper redox centers.
Liu et al. (2014)
5 more

1 mention without citation

X-ray snapshots of possible intermediates in the time course of synthesis and degradation of protein-bound Fe4S4 clusters.
Nicolet et al. (2013)