title: Interactions of the intact FsrC membrane histidine kinase with the tricyclic peptide inhibitor siamycin I revealed through synchrotron radiation circular dichroism.
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.
authors.affiliation: School of Pharmacy and Biomedical Sciences, Faculty of Science and Technology, University of Central Lancashire, Preston, Lancashire, UK. MPhillips-Jones@uclan.ac.uk
authors.forename: Mary K
authors.initials: MK
authors.lastname: Phillips-Jones
authors.forename: Simon G
authors.initials: SG
authors.lastname: Patching
authors.forename: Shalini
authors.initials: S
authors.lastname: Edara
authors.forename: Jiro
authors.initials: J
authors.lastname: Nakayama
authors.forename: Rohanah
authors.initials: R
authors.lastname: Hussain
authors.forename: Giuliano
authors.initials: G
authors.lastname: Siligardi
mesh_terms: D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000037:antagonists & inhibitors* / Q000737:chemistry / Q000378:metabolism*; D002942:Circular Dichroism; D013293:Enterococcus faecalis / Q000737:chemistry / Q000187:drug effects / Q000201:enzymology*; D016908:Gram-Positive Bacterial Infections / Q000382:microbiology; D036341:Intercellular Signaling Peptides and Proteins; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry / Q000494:pharmacology*; D017434:Protein Structure, Tertiary / Q000187:drug effects
chemical_list: C409033:AgrCfs protein, Enterococcus faecalis; D001426:Bacterial Proteins; D036341:Intercellular Signaling Peptides and Proteins; D010455:Peptides; C094260:siamycin I