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.
MeSH terms
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Amino Acid Sequence
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Bacterial Proteins / antagonists & inhibitors*
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Bacterial Proteins / chemistry
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Bacterial Proteins / metabolism*
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Circular Dichroism
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Enterococcus faecalis / chemistry
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Enterococcus faecalis / drug effects
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Enterococcus faecalis / enzymology*
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Gram-Positive Bacterial Infections / microbiology
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Intercellular Signaling Peptides and Proteins
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Molecular Sequence Data
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Peptides / chemistry
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Peptides / pharmacology*
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Protein Structure, Tertiary / drug effects
Substances
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AgrCfs protein, Enterococcus faecalis
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Bacterial Proteins
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Intercellular Signaling Peptides and Proteins
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Peptides
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siamycin I