Transport mechanism of P4 ATPase phosphatidylcholine flippases.
ATP-Binding Cassette Transporters
/ metabolism
Adenosine Triphosphatases
/ metabolism
Adenosine Triphosphate
/ metabolism
Biological Transport, Active
/ physiology
Cell Membrane
/ metabolism
Hydrolysis
Lipid Bilayers
/ metabolism
Membrane Transport Proteins
/ metabolism
P-type ATPases
/ metabolism
Phosphatidylcholines
/ metabolism
Protein Conformation
Saccharomyces cerevisiae
/ enzymology
Saccharomyces cerevisiae Proteins
/ metabolism
P4 ATPase
S. cerevisiae
biochemistry
chemical biology
cryoEM
lipid flippase
lipid transport
molecular biophysics
structural biology
Journal
eLife
ISSN: 2050-084X
Titre abrégé: Elife
Pays: England
ID NLM: 101579614
Informations de publication
Date de publication:
15 12 2020
15 12 2020
Historique:
received:
16
08
2020
accepted:
14
12
2020
pubmed:
16
12
2020
medline:
17
3
2021
entrez:
15
12
2020
Statut:
epublish
Résumé
The P4 ATPases use ATP hydrolysis to transport large lipid substrates across lipid bilayers. The structures of the endosome- and Golgi-localized phosphatidylserine flippases-such as the yeast Drs2 and human ATP8A1-have recently been reported. However, a substrate-binding site on the cytosolic side has not been found, and the transport mechanisms of P4 ATPases with other substrates are unknown. Here, we report structures of the
Identifiants
pubmed: 33320091
doi: 10.7554/eLife.62163
pii: 62163
pmc: PMC7773333
doi:
pii:
Substances chimiques
ATP-Binding Cassette Transporters
0
Lem3 protein, S cerevisiae
0
Lipid Bilayers
0
Membrane Transport Proteins
0
Phosphatidylcholines
0
Saccharomyces cerevisiae Proteins
0
Adenosine Triphosphate
8L70Q75FXE
Adenosine Triphosphatases
EC 3.6.1.-
Dnf2 protein, S cerevisiae
EC 3.6.1.3
P-type ATPases
EC 3.6.3.-
Dnf1 protein, S cerevisiae
EC 7.6.2.1
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : NIDDK NIH HHS
ID : P30 DK058404
Pays : United States
Organisme : NCI NIH HHS
ID : R01 CA231466
Pays : United States
Organisme : NCI NIH HHS
ID : P30 CA068485
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM107978
Pays : United States
Informations de copyright
© 2020, Bai et al.
Déclaration de conflit d'intérêts
LB, QY, BJ, HD, AK, TG, HL No competing interests declared
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