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

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 demons...

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Veröffentlicht in:	Physical chemistry chemical physics : PCCP 2013-01, Vol.15 (2), p.444-447
Hauptverfasser:	Phillips-Jones, Mary K, Patching, Simon G, Edara, Shalini, Nakayama, Jiro, Hussain, Rohanah, Siligardi, Giuliano
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Bacterial Proteins - antagonists & inhibitors Bacterial Proteins - chemistry Bacterial Proteins - metabolism Circular Dichroism Circularity Dichroism Enterococcus faecalis - chemistry Enterococcus faecalis - drug effects Enterococcus faecalis - enzymology Gram-Positive Bacterial Infections - microbiology Histidine Inhibitors Kinases Membranes Molecular Sequence Data Peptides Peptides - chemistry Peptides - pharmacology Protein Structure, Tertiary - drug effects Synchrotron radiation
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Zusammenfassung:	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.
ISSN:	1463-9076 1463-9084
DOI:	10.1039/c2cp43722h