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

Microbiology

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

20 Scopus citations

Abstract

Background: A sex pheromone system controls bacterial conjugation. Results: The initial receptor PrgZ has been crystallized in complex with the sex pheromone cCF10. Conclusion: An extensive network of hydrogen bonds explains the high peptide specificity of PrgZ. Significance: The sex pheromone and inhibitor peptide compete for binding to PrgZ, providing new insight into the regulation of conjugation.

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

Publisher link

10.1074/jbc.M112.386334

Find It

Find It at U of M Libraries

Cite this

@article{23b99bef9be5480c8331551a5400fa1b,

title = "Structure and mode of peptide binding of pheromone receptor PrgZ",

abstract = "Background: A sex pheromone system controls bacterial conjugation. Results: The initial receptor PrgZ has been crystallized in complex with the sex pheromone cCF10. Conclusion: An extensive network of hydrogen bonds explains the high peptide specificity of PrgZ. Significance: The sex pheromone and inhibitor peptide compete for binding to PrgZ, providing new insight into the regulation of conjugation.",

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

year = "2012",

month = oct,

day = "26",

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

language = "English (US)",

volume = "287",

pages = "37165--37170",

journal = "Journal of Biological Chemistry",

issn = "0021-9258",

publisher = "American Society for Biochemistry and Molecular Biology Inc.",

number = "44",

}

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 - Background: A sex pheromone system controls bacterial conjugation. Results: The initial receptor PrgZ has been crystallized in complex with the sex pheromone cCF10. Conclusion: An extensive network of hydrogen bonds explains the high peptide specificity of PrgZ. Significance: The sex pheromone and inhibitor peptide compete for binding to PrgZ, providing new insight into the regulation of conjugation.

AB - Background: A sex pheromone system controls bacterial conjugation. Results: The initial receptor PrgZ has been crystallized in complex with the sex pheromone cCF10. Conclusion: An extensive network of hydrogen bonds explains the high peptide specificity of PrgZ. Significance: The sex pheromone and inhibitor peptide compete for binding to PrgZ, providing new insight into the regulation of conjugation.

UR - https://www.scopus.com/pages/publications/84868257136

UR - https://www.scopus.com/pages/publications/84868257136#tab=citedBy

U2 - 10.1074/jbc.M112.386334

DO - 10.1074/jbc.M112.386334

M3 - Article

C2 - 22948145

AN - SCOPUS:84868257136

SN - 0021-9258

VL - 287

SP - 37165

EP - 37170

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

IS - 44

ER -

Structure and mode of peptide binding of pheromone receptor PrgZ

Abstract

Publisher link

Find It

Other files and links

Fingerprint

Cite this