Abstract
We present the crystal structure of the pheromone receptor protein PrgZ from Enterococcus faecalis in complex with the heptapeptide cCF10 (LVTLVFV), which is used in signaling between conjugative recipient and donor cells. Comparison of PrgZ with homologous oligopeptide-binding proteins (AppA and OppA) explains the high specificity of PrgZ for hydrophobic heptapeptides versus the promiscuity of peptide binding in the homologous proteins.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Bacterial Proteins / chemistry*
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Binding Sites
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Calorimetry, Differential Scanning
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Carrier Proteins / chemistry*
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Crystallography, X-Ray
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Enterococcus faecalis*
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Hydrogen Bonding
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Hydrophobic and Hydrophilic Interactions
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Models, Molecular
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Oligopeptides / chemistry*
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Pheromones / chemistry*
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Protein Binding
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Protein Interaction Domains and Motifs
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Structural Homology, Protein
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Transition Temperature
Substances
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Bacterial Proteins
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Carrier Proteins
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Oligopeptides
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Pheromones
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PrgZ protein, Enterococcus faecalis
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peptide pheromone cCF10