Disease relevance of surA

• We report here the use of a folding method using an immobilized chaperone fragment, a protein disulphide isomerase, and a peptidyl-prolyl cis-trans isomerase (oxidative refolding chromatography) for the fast and efficient assembly of ligand-free and ligand-associated CD1a and CD1b, starting with material synthesized in Escherichia coli [1].
• NMR solution structure and dynamics of the peptidyl-prolyl cis-trans isomerase domain of the trigger factor from Mycoplasma genitalium compared to FK506-binding protein [2].

High impact information on surA

• Cyclophilin (CyP), a major cytosolic protein possessing peptidyl-prolyl cis-trans isomerase activity, has been implicated as the specific receptor of the immunosuppressive drug cyclosporin A (CsA) [3].
• Complementation of UTI89 surA::kan with a plasmid (pDH15) containing surA under the control of an arabinose-inducible promoter restored in vivo binding and invasion events [4].
• Invasion into bladder epithelial cells was disproportionately reduced when surA was genetically disrupted in the UPEC strain UTI89, demonstrating that binding alone is not sufficient for invasion [4].
• The Escherichia coli trigger factor is a peptidyl-prolyl cis-trans isomerase that catalyzes proline-limited protein folding extremely well [5].
• Coexpression of potential folding aids like peptidyl-prolyl cis-trans isomerase or disulfide isomerase does not lead to an increase of soluble enzyme, either when overexpressed separately or from an operon [6].

Analytical, diagnostic and therapeutic context of surA

• Sequence analysis shows that trigger factor contains a domain belonging to the FK506-binding protein (FKBP) family and possessing all the amino acids necessary for FK506 binding and peptidyl-prolyl cis-trans isomerase (Ppiase) activity [7].
• The Escherichia coli peptidyl-prolyl cis-trans isomerase PpiB was expressed in this system with dual amino acid-selective isotope labeling to identify the NMR signal from the active site-residue Arg87 [8].

References