Interactions of the intact FsrC membrane histidine kinase with the tricyclic peptide inhibitor siamycin I revealed through synchrotron radiation circular dichroism

Phys Chem Chem Phys. 2013 Jan 14;15(2):444-7. doi: 10.1039/c2cp43722h. Epub 2012 Nov 26.

Abstract

The suitability of synchrotron radiation circular dichroism spectroscopy (SRCD) for studying interactions between the tricyclic peptide inhibitor siamycin I and the intact FsrC membrane sensor kinase in detergent micelles has been established. In the present study, tertiary structural changes demonstrate that inhibitor binding occurs at a different, non-overlapping site to the native ligand, GBAP.

MeSH terms

  • Amino Acid Sequence
  • Bacterial Proteins / antagonists & inhibitors*
  • Bacterial Proteins / chemistry
  • Bacterial Proteins / metabolism*
  • Circular Dichroism
  • Enterococcus faecalis / chemistry
  • Enterococcus faecalis / drug effects
  • Enterococcus faecalis / enzymology*
  • Gram-Positive Bacterial Infections / microbiology
  • Intercellular Signaling Peptides and Proteins
  • Molecular Sequence Data
  • Peptides / chemistry
  • Peptides / pharmacology*
  • Protein Structure, Tertiary / drug effects

Substances

  • AgrCfs protein, Enterococcus faecalis
  • Bacterial Proteins
  • Intercellular Signaling Peptides and Proteins
  • Peptides
  • siamycin I