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

Mary K. Phillips-Jones; Simon G. Patching; Shalini Edara; Jiro Nakayama; Rohanah Hussain; Giuliano Siligardi

doi:10.1039/c2cp43722h

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

Mary K. Phillips-Jones, Simon G. Patching, Shalini Edara, Jiro Nakayama, Rohanah Hussain, Giuliano Siligardi

Systems Biology

Research output: Contribution to journal › Article › peer-review

10 Citations (Scopus)

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.

Original language	English
Pages (from-to)	444-447
Number of pages	4
Journal	Physical Chemistry Chemical Physics
Volume	15
Issue number	2
DOIs	https://doi.org/10.1039/c2cp43722h
Publication status	Published - Jan 14 2013

All Science Journal Classification (ASJC) codes

Physics and Astronomy(all)
Physical and Theoretical Chemistry

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10.1039/c2cp43722h

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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. / Phillips-Jones, Mary K.; Patching, Simon G.; Edara, Shalini; Nakayama, Jiro; Hussain, Rohanah; Siligardi, Giuliano.

In: Physical Chemistry Chemical Physics, Vol. 15, No. 2, 14.01.2013, p. 444-447.

Research output: Contribution to journal › Article › peer-review

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