› 4edi

X-ray diffraction
2Å resolution

Disulfide bonded EutL from Clostridium perfringens

Released:
DOI: 10.2210/pdb4edi/pdb
PDB entry 4edi coloured by chain, front view.
PDB entry 4edi coloured by chain, side view.
PDB entry 4edi coloured by chain, top view.
Source organism: Clostridium perfringens
Primary publication:
An allosteric model for control of pore opening by substrate binding in the EutL microcompartment shell protein.
Thompson MC, Cascio D, Leibly DJ, Yeates TO
Protein Sci 24 956-75 (2015)
PMID: 25752492

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-186900 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Bacterial microcompartment shell protein EutL Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 225 amino acids
Theoretical weight: 23.72 KDa
Source organism: Clostridium perfringens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q8XLZ0 (Residues: 1-217; Coverage: 100%)
Gene names: CPE0900, eutL
Sequence domains: BMC domain

Ligands and Environments

1 bound ligand:
Ligand NA 1 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-C
Spacegroup: P43212
Unit cell:
a: 86.747Å b: 86.747Å c: 251.681Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.172 0.17 0.193
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

10 review citations

Bacterial microcompartments.
Kerfeld et al. (2018)
9 more

4 mentions without citation

An allosteric model for control of pore opening by substrate binding in the EutL microcompartment shell protein.
Thompson et al. (2015)
3 more