› 2ko7

Solution NMR

Solution structure of peptidyl-prolyl cis-trans isomerase from Burkholderia pseudomallei complexed with Cycloheximide-N-ethylethanoate

Released:
DOI: 10.2210/pdb2ko7/pdb
PDB entry 2ko7 coloured by chain, ensemble of 20 models, front view.
PDB entry 2ko7 coloured by chain, ensemble of 20 models, side view.
PDB entry 2ko7 coloured by chain, ensemble of 20 models, top view.
Source organism: Burkholderia pseudomallei
Primary publication:
The structure of a Burkholderia pseudomallei immunophilin-inhibitor complex reveals new approaches to antimicrobial development.
Norville IH, O'Shea K, Sarkar-Tyson M, Zheng S, Titball RW, Varani G, Harmer NJ
Biochem J 437 413-22 (2011)
PMID: 21574961

Function and Biology Details

Reaction catalysed: 
Peptidylproline (omega=180) = peptidylproline (omega=0)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-179051 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptidyl-prolyl cis-trans isomerase Chain: A
Molecule details ›
Chain: A
Length: 117 amino acids
Theoretical weight: 12.24 KDa
Source organism: Burkholderia pseudomallei
Expression system: Escherichia coli
UniProt:
  • Canonical: Q63J95 (Residues: 1-113; Coverage: 100%)
Gene names: BPSS1823, fbp
Sequence domains: FKBP-type peptidyl-prolyl cis-trans isomerase
Structure domains: Chitinase A; domain 3

Ligands and Environments

1 bound ligand:
Ligand JZF 1 x JZF
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: distance geometry
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Microbial peptidyl-prolyl cis/trans isomerases (PPIases): virulence factors and potential alternative drug targets.
Ünal et al. (2014)
2 more

3 mentions without citation

Novel Cycloheximide Derivatives Targeting the Moonlighting Protein Mip Exhibit Specific Antimicrobial Activity Against Legionella pneumophila.
Rasch et al. (2015)
2 more