Structure of dual BON-domain protein DolP identifies phospholipid binding as a new mechanism for protein localisation.
Anti-Bacterial Agents
/ metabolism
Bacterial Outer Membrane Proteins
/ metabolism
Cell Membrane
/ metabolism
Cell Wall
/ metabolism
Escherichia coli
/ metabolism
Escherichia coli Proteins
/ metabolism
Gram-Negative Bacteria
/ metabolism
Lipoproteins
/ metabolism
Protein Transport
/ physiology
Virulence Factors
/ metabolism
BON domain
E. coli
Escherichia coli
YraP
biochemistry
cell division
chemical biology
infectious disease
microbiology
phospholipids
Journal
eLife
ISSN: 2050-084X
Titre abrégé: Elife
Pays: England
ID NLM: 101579614
Informations de publication
Date de publication:
14 12 2020
14 12 2020
Historique:
received:
31
08
2020
accepted:
11
12
2020
pubmed:
15
12
2020
medline:
10
4
2021
entrez:
14
12
2020
Statut:
epublish
Résumé
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 and function. Here, we reveal DolP is a lipoprotein functionally conserved amongst Gram-negative bacteria and that loss of DolP increases membrane fluidity. We present the NMR solution structure for
Identifiants
pubmed: 33315009
doi: 10.7554/eLife.62614
pii: 62614
pmc: PMC7806268
doi:
pii:
Substances chimiques
Anti-Bacterial Agents
0
Bacterial Outer Membrane Proteins
0
Escherichia coli Proteins
0
Lipoproteins
0
Virulence Factors
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : Natural Sciences and Engineering Research Council of Canada
ID : RCP-12-002C
Pays : International
Organisme : Biotechnology and Biological Sciences Research Council
ID : BB/M00810X/1
Pays : United Kingdom
Organisme : Biotechnology and Biological Sciences Research Council
ID : BB/L00335X/1
Pays : United Kingdom
Organisme : Biotechnology and Biological Sciences Research Council
ID : BB/P009840/1
Pays : United Kingdom
Organisme : Campus Alberta Neuroscience
ID : RCP-12-002C
Pays : International
Organisme : Natural Sciences and Engineering Research Council of Canada
ID : RGPIN-2018-04994
Pays : International
Informations de copyright
© 2020, Bryant et al.
Déclaration de conflit d'intérêts
JB, FM, TK, RM, EH, GB, DA, AC, PW, KS, MJ, DB, YS, TW, AR, VB, PS, DW, ZC, EG, CI, AT, SC, DR, TL, AC, MB, MO, IH No competing interests declared
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