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 Sep 4;9(10):1697–1708. doi: 10.1038/s41477-023-01510-0

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. 4 — a, Overview of the electron density for the ABCG25 E232Q mutant in the ATP-bound state. Densities corresponding to the ABCG25 monomers are coloured blue and green. The detergent density is shown in grey. b, Overall structure of the ATP-bound ABCG25_EQ and the EM density for the ATP molecule (with nitrogen and phosphorus atoms coloured magenta and orange, respectively) and magnesium (coloured red). c, Coordination of ATP and Mg²⁺ by ABCG25. The ATP molecule and interacting residues are shown as sticks in the zoom-in views. Hydrogen bonds are shown as red dashed lines. d, Section view of the surface electrostatic potential of the ATP-bound ABCG25_EQ (left) and a cartoon representation of the NBDs with the ATP-binding site (right). e, Structure alignments of ABCG25_EQ, hABCG1_EQ (PDB code: 7R8E) and hABCG2_EQ (PDB code: 6HBU) in the ATP-bound state. ABCG25, hABCG1 and hABCG2 are coloured grey, green and pink, respectively. f, Comparison of the TMDs of the ABA-bound ABCG25_WT (coloured orange) and the ATP-bound ABCG25_EQ (coloured grey) structures.