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Solution NMR

Structural Basis of a Thiopeptide Antibiotic Multidrug Resistance System from Streptomyces lividans:Promothiocin A in Complex with TipAS

Released:
DOI: 10.2210/pdb2mbz/pdb
PDB entry 2mbz coloured by chain, ensemble of 10 models, front view.
PDB entry 2mbz coloured by chain, ensemble of 10 models, side view.
PDB entry 2mbz coloured by chain, ensemble of 10 models, top view.
Source organisms:
Primary publication:
Structural basis and dynamics of multidrug recognition in a minimal bacterial multidrug resistance system.
Habazettl J, Allan M, Jensen PR, Sass HJ, Thompson CJ, Grzesiek S
Proc Natl Acad Sci U S A 111 E5498-507 (2014)
PMID: 25489067

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141265 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
HTH-type transcriptional activator TipA Chain: A
Molecule details ›
Chain: A
Length: 144 amino acids
Theoretical weight: 16.58 KDa
Source organism: Streptomyces lividans
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A4T9 (Residues: 110-253; Coverage: 57%)
Gene name: tipA
Sequence domains: TipAS antibiotic-recognition domain
Promothiocin A Chain: B
Molecule details ›
Chain: B
Length: 12 amino acids
Theoretical weight: 942 Da
Source organism: synthetic construct
Expression system: Not provided

Ligands and Environments

No bound ligands
1 modified residue:
Ligand BB9 2 x BB9

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 89%
Refinement method: simulated annealing
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

2 review citations

YcaO-Dependent Posttranslational Amide Activation: Biosynthesis, Structure, and Function.
Burkhart et al. (2017)
1 more

3 mentions without citation

Mechanism of Action of Ribosomally Synthesized and Post-Translationally Modified Peptides.
Ongpipattanakul et al. (2022)
2 more