8H1D

Solid-state NMR Structure of Aquaporin Z in its Native Cellular Membranes

Summary for 8H1D

• Entry DOI: 10.2210/pdb8h1d/pdb
• Descriptor: Aquaporin Z (1 entity in total)
• Functional Keywords: membrane protein
• Biological source: Escherichia coli BL21(DE3)
• Total number of polymer chains: 1
• Total formula weight: 25185.24

Authors

Xie, H.,Zhao, Y.,Zhao, W.,Chen, Y.,Liu, M.,Yang, J. (deposition date: 2022-10-02, release date: 2022-11-09, Last modification date: 2024-05-15)

Primary citation

Xie, H.,Zhao, Y.,Zhao, W.,Chen, Y.,Liu, M.,Yang, J.
Solid-state NMR structure determination of a membrane protein in E. coli cellular inner membrane.
Sci Adv, 9:eadh4168-eadh4168, 2023

PubMed Abstract: Structure determination of membrane proteins in native cellular membranes is critical to precisely reveal their structures in physiological conditions. However, it remains challenging for solid-state nuclear magnetic resonance (ssNMR) due to the low sensitivity and high complexity of ssNMR spectra of cellular membranes. Here, we present the structure determination of aquaporin Z (AqpZ) by ssNMR in inner membranes. To enhance the signal sensitivity of AqpZ, we optimized protein overexpression and removed outer membrane components. To suppress the interference of background proteins, we used a "dual-media" expression approach and antibiotic treatment. Using 1017 distance restraints obtained from two-dimensional C-C spectra based on the complete chemical shift assignments, the 1.7-Å ssNMR structure of AqpZ is determined in inner membranes. This cellular ssNMR structure determination paves the way for analyzing the atomic structural details for membrane proteins in native cellular membranes.

PubMed: 37910616
DOI: 10.1126/sciadv.adh4168

Experimental method

SOLID-STATE NMR