› 4do2

X-ray diffraction
1.4Å resolution

Crystal Structure of the Rop protein mutant D30P/A31G at resolution 1.4 resolution.

Released:
DOI: 10.2210/pdb4do2/pdb
PDB entry 4do2 coloured by chain, front view.
PDB entry 4do2 coloured by chain, side view.
PDB entry 4do2 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Structural plasticity of 4-α-helical bundles exemplified by the puzzle-like molecular assembly of the Rop protein.
Amprazi M, Kotsifaki D, Providaki M, Kapetaniou EG, Fellas G, Kyriazidis I, Pérez J, Kokkinidis M
Proc Natl Acad Sci U S A 111 11049-54 (2014)
PMID: 25024213

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-136490 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Regulatory protein rop Chains: A, B
Molecule details ›
Chains: A, B
Length: 70 amino acids
Theoretical weight: 8.16 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P03051 (Residues: 1-63; Coverage: 100%)
Gene name: rop
Sequence domains: Rop protein
Structure domains: Helix Hairpins

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X11
Spacegroup: P21
Unit cell:
a: 26.669Å b: 38.823Å c: 56.644Å
α: 90° β: 100.87° γ: 90°
R-values:
R R work R free
0.16 0.159 0.188
Expression system: Escherichia coli

Quick links

Citations

1 review citation

α-Helices in the Type III Secretion Effectors: A Prevalent Feature with Versatile Roles.
Gazi et al. (2021)
6 other articles

3 mentions without citation

De novo design of covalently constrained mesosize protein scaffolds with unique tertiary structures.
Dang et al. (2017)
2 more