› 1tlv

X-ray diffraction
1.95Å resolution

Structure of the native and inactive LicT PRD from B. subtilis

Released:
DOI: 10.2210/pdb1tlv/pdb
PDB entry 1tlv coloured by chain, front view.
PDB entry 1tlv coloured by chain, side view.
PDB entry 1tlv coloured by chain, top view.
Source organism: Bacillus subtilis
Primary publication:
Activation of the LicT transcriptional antiterminator involves a domain swing/lock mechanism provoking massive structural changes.
Graille M, Zhou CZ, Receveur-Bréchot V, Collinet B, Declerck N, van Tilbeurgh H
J Biol Chem 280 14780-9 (2005)
PMID: 15699035

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-153957 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Transcription antiterminator LicT Chain: A
Molecule details ›
Chain: A
Length: 221 amino acids
Theoretical weight: 26.19 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli
UniProt:
  • Canonical: P39805 (Residues: 57-274; Coverage: 79%)
Gene names: BSU39080, N15A, licT
Sequence domains: PRD domain
Structure domains: PRD domain

Ligands and Environments

No bound ligands
1 modified residue:
Ligand CME 1 x CME

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P3221
Unit cell:
a: 48.734Å b: 48.734Å c: 162.472Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.269 0.269 0.292
Expression system: Escherichia coli

Quick links

Citations

12 review citations

Carbon catabolite repression in bacteria: many ways to make the most out of nutrients.
Görke et al. (2008)
11 more

9 mentions without citation

The Landscape of Intertwined Associations in Homooligomeric Proteins.
Wodak et al. (2015)
8 more