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

DOI: 10.1039/c2cp43722h DOI Help

Authors: Mary Phillips-jones (University of Central Lancashire) , Simon Patching (University of Leeds) , Shalini Edara (University of Leeds) , Jiro Nakayama (Kyushu University) , Rohanah Hussain (Diamond Light Source) , Giuliano Siligardi (Diamond Light Source)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Physical Chemistry Chemical Physics , VOL 15 (2) , PAGES 444-447

State: Published (Approved)
Published: January 2013
Diamond Proposal Number(s): 7106

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.

Journal Keywords: Siamycin; SRCD; B23; Membrane Protein; Histidine Kinase

Subject Areas: Biology and Bio-materials, Medicine, Technique Development


Instruments: B23-Circular Dichroism

Other Facilities: No