Structural basis of substrate recognition and translocation by human ABCA4

Structural basis of substrate recognition and translocation by human ABCA4

Here, cryo-EM structures of human retinal ABCA4 transporter, either in apo state, in complex with ATP or with the physiological lipid substrate N-retinylidene-phosphatidylethanolamine (NRPE), reveal lateral opening, substrate recognition and suggest ‘lateral access and extrusion’ mechanism for ABCA-...

Full description

Bibliographic Details
Main Authors: Tian Xie, Zike Zhang, Qi Fang, Bowen Du, Xin Gong
Format: Article
Language:English
Published: Nature Publishing Group 2021-06-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-021-24194-6
id doaj-eb492f4b734c4a06849ad264dacdecf4
record_format Article
spelling doaj-eb492f4b734c4a06849ad264dacdecf42021-06-27T11:12:13ZengNature Publishing GroupNature Communications2041-17232021-06-0112111110.1038/s41467-021-24194-6Structural basis of substrate recognition and translocation by human ABCA4Tian Xie0Zike Zhang1Qi Fang2Bowen Du3Xin Gong4Department of Biology, Southern University of Science and TechnologyDepartment of Biology, Southern University of Science and TechnologyDepartment of Biology, Southern University of Science and TechnologyDepartment of Biology, Southern University of Science and TechnologyDepartment of Biology, Southern University of Science and TechnologyHere, cryo-EM structures of human retinal ABCA4 transporter, either in apo state, in complex with ATP or with the physiological lipid substrate N-retinylidene-phosphatidylethanolamine (NRPE), reveal lateral opening, substrate recognition and suggest ‘lateral access and extrusion’ mechanism for ABCA-mediated lipid transport.https://doi.org/10.1038/s41467-021-24194-6
collection DOAJ
language English
format Article
sources DOAJ
author Tian Xie
Zike Zhang
Qi Fang
Bowen Du
Xin Gong
spellingShingle Tian Xie
Zike Zhang
Qi Fang
Bowen Du
Xin Gong
Structural basis of substrate recognition and translocation by human ABCA4
Nature Communications
author_facet Tian Xie
Zike Zhang
Qi Fang
Bowen Du
Xin Gong
author_sort Tian Xie
title Structural basis of substrate recognition and translocation by human ABCA4
title_short Structural basis of substrate recognition and translocation by human ABCA4
title_full Structural basis of substrate recognition and translocation by human ABCA4
title_fullStr Structural basis of substrate recognition and translocation by human ABCA4
title_full_unstemmed Structural basis of substrate recognition and translocation by human ABCA4
title_sort structural basis of substrate recognition and translocation by human abca4
publisher Nature Publishing Group
series Nature Communications
issn 2041-1723
publishDate 2021-06-01
description Here, cryo-EM structures of human retinal ABCA4 transporter, either in apo state, in complex with ATP or with the physiological lipid substrate N-retinylidene-phosphatidylethanolamine (NRPE), reveal lateral opening, substrate recognition and suggest ‘lateral access and extrusion’ mechanism for ABCA-mediated lipid transport.
url https://doi.org/10.1038/s41467-021-24194-6
work_keys_str_mv AT tianxie structuralbasisofsubstraterecognitionandtranslocationbyhumanabca4
AT zikezhang structuralbasisofsubstraterecognitionandtranslocationbyhumanabca4
AT qifang structuralbasisofsubstraterecognitionandtranslocationbyhumanabca4
AT bowendu structuralbasisofsubstraterecognitionandtranslocationbyhumanabca4
AT xingong structuralbasisofsubstraterecognitionandtranslocationbyhumanabca4
_version_ 1721358202405126144

Similar Items