Unknown

Dataset Information

0

Cryo-EM structures of human P4-ATPase flippase


ABSTRACT:

SUBMITTER: Tomohiro Nishizawa 

PROVIDER: EMPIAR-10303 | biostudies-other |

REPOSITORIES: biostudies-other

altmetric image

Publications

Cryo-EM structures capture the transport cycle of the P4-ATPase flippase.

Hiraizumi Masahiro M   Yamashita Keitaro K   Nishizawa Tomohiro T   Nureki Osamu O  

Science (New York, N.Y.) 20190815 6458


In eukaryotic membranes, type IV P-type adenosine triphosphatases (P4-ATPases) mediate the translocation of phospholipids from the outer to the inner leaflet and maintain lipid asymmetry, which is critical for membrane trafficking and signaling pathways. Here, we report the cryo-electron microscopy structures of six distinct intermediates of the human ATP8A1-CDC50a heterocomplex at resolutions of 2.6 to 3.3 angstroms, elucidating the lipid translocation cycle of this P4-ATPase. ATP-dependent pho  ...[more]

Similar Datasets

| EMPIAR-11132 | biostudies-other
| S-EPMC8564547 | biostudies-literature
| S-EPMC7414150 | biostudies-literature
| S-EPMC7196119 | biostudies-literature
| S-EPMC8408191 | biostudies-literature
| S-EPMC3273382 | biostudies-literature
| S-EPMC6329974 | biostudies-literature
| S-EPMC5777635 | biostudies-literature
| S-EPMC8176766 | biostudies-literature
| S-EPMC6497962 | biostudies-literature