Structure of dual BON-domain protein DolP identifies phospholipid binding as a new mechanism for protein localisation

Structure of dual BON-domain protein DolP identifies phospholipid binding as a new mechanism for protein localisation

The Gram-negative outer-membrane envelops the bacterium and functions as a permeability barrier against antibiotics, detergents, and environmental stresses. Some virulence factors serve to maintain the integrity of the outer membrane, including DolP (formerly YraP) a protein of unresolved structure...

Full description

Bibliographic Details
Main Authors: Jack Alfred Bryant, Faye C Morris, Timothy J Knowles, Riyaz Maderbocus, Eva Heinz, Gabriela Boelter, Dema Alodaini, Adam Colyer, Peter J Wotherspoon, Kara A Staunton, Mark Jeeves, Douglas F Browning, Yanina R Sevastsyanovich, Timothy J Wells, Amanda E Rossiter, Vassiliy N Bavro, Pooja Sridhar, Douglas G Ward, Zhi-Soon Chong, Emily CA Goodall, Christopher Icke, Alvin CK Teo, Shu-Sin Chng, David I Roper, Trevor Lithgow, Adam F Cunningham, Manuel Banzhaf, Michael Overduin, Ian R Henderson
Format: Article
Language:English
Published: eLife Sciences Publications Ltd 2020-12-01
Series:eLife
Subjects:
BON domain
Escherichia coli
YraP
phospholipids
cell division
Online Access:https://elifesciences.org/articles/62614

Internet

https://elifesciences.org/articles/62614

Similar Items