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

. 2022 Nov 17;14(6):448–458. doi: 10.1093/procel/pwac060

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

©The Author(s) 2022. Published by Oxford University Press on behalf of Higher Education Press.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (https://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.

PMC Copyright notice

Figure 3. — The metal ion binding site of IrtAB in the occluded state. (A) Close-up view of the metal ion binding site in the TM region of IrtA. The density map for metal ion and residues that ligand to this metal is shown in mesh. Interactions between histidine and metal ion are indicated by dashed lines. (B) The ATPase activities of two variants in metal ion binding site were normalized relative to that of the wild-type (WT) IrtAB. Error bars represent mean ± SD based on three independent measurements. (C) Representative cryo-EM 2D class averages of IrtAB_ΔSID (E-Q) and two variants in the presence of 10 mmol/L ATP and MgCl₂. (D) Cartoon representation of the structure of IrtA_H407AB_ΔSID (E-Q) in complex with ATP. The density maps for ATP (magenta sticks) and Mg²⁺ (yellow spheres) are shown as grey mesh and contoured at 9 σ. (E) The density map for the metal ion binding site in IrtA_H407A is shown as grey mesh and contoured at 7.5 σ.