› 4b27

X-ray diffraction
2.72Å resolution

Trp RNA-binding attenuation protein: modifying symmetry and stability of a circular oligomer

Released:
DOI: 10.2210/pdb4b27/pdb
PDB entry 4b27 coloured by chain, front view.
PDB entry 4b27 coloured by chain, side view.
PDB entry 4b27 coloured by chain, top view.
Source organism: Bacillus subtilis
Primary publication:
Trp RNA-binding attenuation protein: modifying symmetry and stability of a circular oligomer.
Bayfield OW, Chen CS, Patterson AR, Luan W, Smits C, Gollnick P, Antson AA
PLoS One 7 e44309 (2012)
PMID: 22970197

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dodecamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-148584 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Transcription attenuation protein MtrB Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 75 amino acids
Theoretical weight: 8.37 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P19466 (Residues: 1-75; Coverage: 100%)
Gene names: BSU22770, mtrB
Sequence domains: Tryptophan RNA-binding attenuator protein
Structure domains: TRAP-like

Ligands and Environments

1 bound ligand:
Ligand TRP 6 x TRP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: P21212
Unit cell:
a: 109.467Å b: 110.151Å c: 46.229Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.209 0.207 0.245
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

4 citation in other articles

Tuning the size and properties of ClyA nanopores assisted by directed evolution.
Soskine et al. (2013)
3 more

1 mention without citation

Trp RNA-binding attenuation protein: modifying symmetry and stability of a circular oligomer.
Bayfield et al. (2012)