Structure and Mode of Peptide Binding of Pheromone Receptor PrgZ

Ronnie P. -A. Berntsson; Gea K. Schuurman-Wolters; Gary Dunny; Dirk-Jan Slotboom; Bert Poolman

doi:10.1074/jbc.M112.386334

Structure and Mode of Peptide Binding of Pheromone Receptor PrgZ

Ronnie P. -A. Berntsson
, Gea K. Schuurman-Wolters
, Gary Dunny
, Dirk-Jan Slotboom
, Bert Poolman^*

^*Corresponding author for this work

Enzymology

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

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Abstract

Wepresent 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.

Original language	English
Pages (from-to)	37165-37170
Number of pages	6
Journal	The Journal of Biological Chemistry
Volume	287
Issue number	44
DOIs	https://doi.org/10.1074/jbc.M112.386334
Publication status	Published - 26-Oct-2012

Keywords

FAECALIS PLASMID PCF10
ENTEROCOCCUS-FAECALIS
SEX-PHEROMONE
MACROMOLECULAR STRUCTURES
PROTEIN OPPA
CONJUGATION
EXPRESSION
CCF10
CRYSTALLOGRAPHY
VALIDATION

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title = "Structure and Mode of Peptide Binding of Pheromone Receptor PrgZ",

abstract = "Wepresent 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.",

keywords = "FAECALIS PLASMID PCF10, ENTEROCOCCUS-FAECALIS, SEX-PHEROMONE, MACROMOLECULAR STRUCTURES, PROTEIN OPPA, CONJUGATION, EXPRESSION, CCF10, CRYSTALLOGRAPHY, VALIDATION",

author = "Berntsson, \{Ronnie P. -A.\} and Schuurman-Wolters, \{Gea K.\} and Gary Dunny and Dirk-Jan Slotboom and Bert Poolman",

year = "2012",

month = oct,

day = "26",

doi = "10.1074/jbc.M112.386334",

language = "English",

volume = "287",

pages = "37165--37170",

journal = "The Journal of Biological Chemistry",

issn = "0021-9258",

publisher = "AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC",

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TY - JOUR

T1 - Structure and Mode of Peptide Binding of Pheromone Receptor PrgZ

AU - Berntsson, Ronnie P. -A.

AU - Schuurman-Wolters, Gea K.

AU - Dunny, Gary

AU - Slotboom, Dirk-Jan

AU - Poolman, Bert

PY - 2012/10/26

Y1 - 2012/10/26

N2 - Wepresent 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.

AB - Wepresent 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.

KW - FAECALIS PLASMID PCF10

KW - ENTEROCOCCUS-FAECALIS

KW - SEX-PHEROMONE

KW - MACROMOLECULAR STRUCTURES

KW - PROTEIN OPPA

KW - CONJUGATION

KW - EXPRESSION

KW - CCF10

KW - CRYSTALLOGRAPHY

KW - VALIDATION

U2 - 10.1074/jbc.M112.386334

DO - 10.1074/jbc.M112.386334

M3 - Article

SN - 0021-9258

VL - 287

SP - 37165

EP - 37170

JO - The Journal of Biological Chemistry

JF - The Journal of Biological Chemistry

IS - 44

ER -

Structure and Mode of Peptide Binding of Pheromone Receptor PrgZ

Abstract

Keywords

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