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 - http://www.scopus.com/inward/record.url?scp=84868257136&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84868257136&partnerID=8YFLogxK
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 -