› 1wap

X-ray diffraction
1.8Å resolution

TRP RNA-BINDING ATTENUATION PROTEIN IN COMPLEX WITH L-TRYPTOPHAN

Released:
DOI: 10.2210/pdb1wap/pdb
PDB entry 1wap coloured by chain, front view.
PDB entry 1wap coloured by chain, side view.
PDB entry 1wap coloured by chain, top view.
Source organism: Bacillus subtilis
Primary publication:
The structure of trp RNA-binding attenuation protein.
Antson AA, Otridge J, Brzozowski AM, Dodson EJ, Dodson GG, Wilson KS, Smith TM, Yang M, Kurecki T, Gollnick P
Nature 374 693-700 (1995)
PMID: 7715723

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo undecamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-148583 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Transcription attenuation protein MtrB Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V
Length: 75 amino acids
Theoretical weight: 8.34 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli
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 22 x TRP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X11
Spacegroup: C2
Unit cell:
a: 155.91Å b: 114.44Å c: 105.67Å
α: 90° β: 117.64° γ: 90°
R-values:
R R work R free
0.178 0.178 0.225
Expression system: Escherichia coli

Quick links

Citations

26 review citations

Themes in RNA-protein recognition.
Draper DE. (1999)
25 more

9 mentions without citation

Overview of protein structural and functional folds.
Sun et al. (2004)
8 more