8VI4

TehA from Haemophilus influenzae purified in LMNG

Summary for 8VI4

• Entry DOI: 10.2210/pdb8vi4/pdb
• EMDB information: 43248
• Descriptor: Tellurite resistance protein TehA homolog (1 entity in total)
• Functional Keywords: anion channel, alpha helical integral membrane protein, membrane protein
• Biological source: Haemophilus influenzae
• Total number of polymer chains: 3
• Total formula weight: 105757.64

Authors

Catalano, C.,Senko, S.,Tran, N.L.,Lucier, K.W.,Farwell, A.C.,Silva, M.S.,Dip, P.V.,Poweleit, N.,Scapin, G. (deposition date: 2024-01-03, release date: 2024-05-08)

Primary citation

Tran, N.L.,Senko, S.,Lucier, K.W.,Farwell, A.C.,Silva, S.M.,Dip, P.V.,Poweleit, N.,Scapin, G.,Catalano, C.
High-Resolution Cryo-Electron Microscopy Structure Determination of Haemophilus influenzae Tellurite-Resistance Protein A via 200 kV Transmission Electron Microscopy.
Int J Mol Sci, 25:-, 2024

PubMed Abstract: Membrane proteins constitute about 20% of the human proteome and play crucial roles in cellular functions. However, a complete understanding of their structure and function is limited by their hydrophobic nature, which poses significant challenges in purification and stabilization. Detergents, essential in the isolation process, risk destabilizing or altering the proteins' native conformations, thus affecting stability and functionality. This study leverages single-particle cryo-electron microscopy to elucidate the structural nuances of membrane proteins, focusing on the SLAC1 bacterial homolog from (TehA) purified with diverse detergents, including n-dodecyl β-D-maltopyranoside (DDM), glycodiosgenin (GDN), β-D-octyl-glucoside (OG), and lauryl maltose neopentyl glycol (LMNG). This research not only contributes to the understanding of membrane protein structures but also addresses detergent effects on protein purification. By showcasing that the overall structural integrity of the channel is preserved, our study underscores the intricate interplay between proteins and detergents, offering insightful implications for drug design and membrane biology.

PubMed: 38674110
DOI: 10.3390/ijms25084528

Experimental method

ELECTRON MICROSCOPY (3.1 Å)