› 1qx8

X-ray diffraction
2.02Å resolution

Crystal structure of a five-residue deletion mutant of the Rop protein

Released:
DOI: 10.2210/pdb1qx8/pdb
PDB entry 1qx8 coloured by chain, front view.
PDB entry 1qx8 coloured by chain, side view.
PDB entry 1qx8 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Loopless Rop: structure and dynamics of an engineered homotetrameric variant of the repressor of primer protein.
Glykos NM, Papanikolau Y, Vlassi M, Kotsifaki D, Cesareni G, Kokkinidis M
Biochemistry 45 10905-19 (2006)
PMID: 16953576

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-136492 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Regulatory protein rop Chains: A, B
Molecule details ›
Chains: A, B
Length: 58 amino acids
Theoretical weight: 6.68 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P03051 (Residues: 1-63; Coverage: 92%)
Gene name: rop
Sequence domains: Rop protein
Structure domains: Regulatory protein rop

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: C2
Unit cell:
a: 54.476Å b: 42.565Å c: 51.722Å
α: 90° β: 104.68° γ: 90°
R-values:
R R work R free
0.191 0.189 0.212
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Coiled-coils in type III secretion systems: structural flexibility, disorder and biological implications.
Gazi et al. (2009)
1 more

6 mentions without citation

Simultaneous prediction of protein folding and docking at high resolution.
Das et al. (2009)
5 more