Figure - PMC

Skip to main content

An official website of the United States government

Here's how you know

Here's how you know

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS
A lock ( ) or https:// means you've safely connected to the .gov website. Share sensitive information only on official, secure websites.

View full-text article in PMC

. 2023 May 8;14:2571. doi: 10.1038/s41467-023-37702-7

Search in PMC
Search in PubMed
View in NLM Catalog
Add to search

© The Author(s) 2023

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

PMC Copyright notice

Fig. 1 — a The preferred Mfsd2a DHA-LPC substrate and the ALA-LPC ligand observed in the drMfsd2a structures. b Overall architecture of drMfsd2a with the N-terminal domain, TM1-6, in blue and the C-terminal domain, TM7-12, in wheat. c Extracellular view of the substrate translocation pathway with the overlay of the four lysolipid positions observed in drMfsd2a. Dashed lines represent the proposed transport path of the C18 of the lipid tail through a cleft between the N- and C-domains. d Cytoplasmic view of the substrate translocation pathway with the overlay of the four lipid positions observed in drMfsd2a through a cleft between the N- and C-domains. Dashed lines represent the proposed transport path of the choline of the LPC headgroup. b–d Ligands illustrated as stick and sphere. e The ligand-free and the four elongated lipid-like densities fitted with ALA-LPC observed for drMfsd2a starting from the position closest to the extracellular towards the cytoplasmic side. Protein rendered as gray cartoon. Elongated densities shown as gray mesh. Lipid isomerism cannot be ascertained at the current resolution.