Structure of peptide sex pheromone receptor PrgX and PrgX/pheromone complexes and regulation of conjugation in Enterococcus faecalis

Ke Shi, C. Kent Brown, Zu Yi Gu, Briana K. Kozlowicz, Gary M. Dunny, Douglas H. Ohlendorf, Cathleen A. Earhart

Research output: Contribution to journalArticlepeer-review

95 Scopus citations

Abstract

Many bacterial activities, including expression of virulence factors, horizontal genetic transfer, and production of antibiotics, are controlled by intercellular signaling using small molecules. To date, understanding of the molecular mechanisms of peptide-mediated cell-cell signaling has been limited by a dearth of published information about the molecular structures of the signaling components. Here, we present the molecular structure of PrgX, a DNA-and peptide-binding protein that regulates expression of the conjugative transfer genes of the Enterococcus faecalis plasmid pCF10 in response to an intercellular peptide pheromone signal. Comparison of the structures of PrgX and the PrgX/pheromone complex suggests that pheromone binding destabilizes PrgX tetramers, opening a 70-bp pCF10 DNA loop required for conjugation repression.

Original languageEnglish (US)
Pages (from-to)18596-18601
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume102
Issue number51
DOIs
StatePublished - Dec 20 2005

Keywords

  • DNA binding
  • Gram-positive bacteria
  • Inducible conjugation
  • Transcription factor
  • X-ray crystallography

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