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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

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Phillips-Jones, Mary ORCID: 0000-0002-0362-4690, Patching, Simon G., Edara, Shalini, Nakayama, Jiro, Hussain, Rohanah and Siligardi, Giuliano (2013) Interactions of the intact FsrC membrane histidine kinase with the tricyclic peptide inhibitor siamycin I revealed through synchrotron radiation circular dichroism. Physical Chemistry Chemical Physics, 15 (2). pp. 444-447. ISSN 1463-9076

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Official URL: http://dx.doi.org/10.1039/c2cp43722h

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.

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