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

. 2025 Aug 4;11(8):1670–1680. doi: 10.1038/s41477-025-02056-z

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

© The Author(s) 2025

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 licence, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons licence 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 licence, visit http://creativecommons.org/licenses/by/4.0/.

PMC Copyright notice

Extended Data Fig. 8 — a. The model of LAX3 (cartoons) bound to IAA (orange) was submitted to ConSurf and colored according to the degree of residue conservation as blue (least conserved), white (moderately conserved) or maroon (highly conserved). Two close-up views of the amino acids in the binding pocket as sticks show that they are highly conserved. b. Structures of sodium-independent transporters of auxin (LAX), amino acids (ApcT) and carnitine (CaiT) are compared with a sodium-dependent transporter of amino acids (LeuT). Models are shown as grey cartoons while helices that contribute residues to site 1 or site 2 are colored green (M1 and M6 of the bundle domain), orange (M5 of the scaffold domain) and light purple (M8 scaffold domain). The location of site 1 and site 2 are shown in cyan and yellow circles, respectively. Key residues involved in charge stabilization of the sodium-independent transporters are shown in blue or red, while the two sodium ions that fulfill the same role in the sodium-dependent LeuT protein are also shown in blue and red. c. Superposition of helices M1, M5, M6 and M8 of LAX3 (dark blue), ApcT (light blue), LeuT (pink) and CaiT (light green). For both the side and top view, the location of site 1 and site 2 are shown with a cyan and yellow circle, respectively, as well as the sodium ions coordinated by LeuT.