2zp8

X-ray diffraction
3.2Å resolution

The Nature of the TRAP:Anti-TRAP complex

Released:
Primary publication:
The nature of the TRAP-Anti-TRAP complex.
Proc Natl Acad Sci U S A 106 2176-81 (2009)
PMID: 19164760

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero 30-mer (preferred)
PDBe Complex ID:
PDB-CPX-128292 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Transcription attenuation protein MtrB Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 74 amino acids
Theoretical weight: 8.26 KDa
Source organism: Geobacillus stearothermophilus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9X6J6 (Residues: 1-74; Coverage: 100%)
Gene name: mtrB
Sequence domains: Tryptophan RNA-binding attenuator protein
Structure domains: TRAP-like
Tryptophan RNA-binding attenuator protein inhibitory protein Chains: E, F, G, H, I, J
Molecule details ›
Chains: E, F, G, H, I, J
Length: 53 amino acids
Theoretical weight: 5.66 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli
UniProt:
  • Canonical: O31466 (Residues: 1-53; Coverage: 100%)
Gene names: BSU02530, rtpA, yczA
Sequence domains: Tryptophan RNA-binding attenuator protein inhibitory protein
Structure domains: Chaperone, DNAj Protein; Chain A

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-17A
Spacegroup: R32
Unit cell:
a: 201.134Å b: 201.134Å c: 133.168Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.231 0.229 0.268
Expression system: Escherichia coli