2GRL

Crystal structure of dCT/iCF10 complex

Summary for 2GRL

• Entry DOI: 10.2210/pdb2grl/pdb
• Related: 2GRM
• Descriptor: PrgX, peptide (3 entities in total)
• Functional Keywords: receptor, inhibitor, transcription
• Biological source: Enterococcus faecalis
• Total number of polymer chains: 5
• Total formula weight: 149340.19

Authors

Shi, K.,Kozlowicz, B.K.,Gu, Z.Y.,Ohlendorf, D.H.,Earhart, C.A.,Dunny, G.M. (deposition date: 2006-04-24, release date: 2007-04-03, Last modification date: 2024-02-14)

Primary citation

Kozlowicz, B.K.,Shi, K.,Gu, Z.Y.,Ohlendorf, D.H.,Earhart, C.A.,Dunny, G.M.
Molecular basis for control of conjugation by bacterial pheromone and inhibitor peptides.
Mol.Microbiol., 62:958-969, 2006

PubMed Abstract: In many bacteria expression of lateral gene transfer and of virulence factors is controlled by cell-cell signalling systems. Molecular interactions of microbial signal molecules with their cognate receptors are not well understood. For the Enterococcus faecalis conjugative plasmid pCF10, the PrgX protein serves as a molecular switch controlling expression of conjugation and virulence genes encoded by the plasmid. The induction state of a pCF10-carrying donor cell is determined by the ratio of two signalling peptides, cCF10 pheromone and iCF10 inhibitor. Recent analysis of PrgX/cCF10 interactions suggests a mechanism for conversion to the induced state. However, the means by which iCF10 peptide antagonizes cCF10 activity is unclear, and it has been suggested that inhibitor peptides block import of pheromone peptides. We now show that both of these peptides interact with the same binding pocket of PrgX, but they differentially alter the conformation of the protein and its oligomerization state, resulting in opposing biological activities.

PubMed: 17038121
DOI: 10.1111/j.1365-2958.2006.05434.x

Experimental method

X-RAY DIFFRACTION (3 Å)