Issue 2, 2013

Interactions of the intact FsrC membrane histidine kinase with the tricyclic peptideinhibitor 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.

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

Supplementary files

Article information

Article type
Communication
Submitted
22 Oct 2012
Accepted
13 Nov 2012
First published
14 Nov 2012

Phys. Chem. Chem. Phys., 2013,15, 444-447

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

M. K. Phillips-Jones, S. G. Patching, S. Edara, J. Nakayama, R. Hussain and G. Siligardi, Phys. Chem. Chem. Phys., 2013, 15, 444 DOI: 10.1039/C2CP43722H

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