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TitleHigh-Resolution Cryo-Electron Microscopy Structure Determination of Tellurite-Resistance Protein A via 200 kV Transmission Electron Microscopy.
Journal, issue, pagesInt J Mol Sci, Vol. 25, Issue 8, Year 2024
Publish dateApr 20, 2024
AuthorsNhi L Tran / Skerdi Senko / Kyle W Lucier / Ashlyn C Farwell / Sabrina M Silva / Phat V Dip / Nicole Poweleit / Giovanna Scapin / Claudio Catalano /
PubMed AbstractMembrane 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 ...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.
External linksInt J Mol Sci / PubMed:38674110 / PubMed Central
MethodsEM (single particle)
Resolution2.9 - 3.2 Å
Structure data

43246

8vi2

EMDB-43246, PDB-8vi2:
TehA from Haemophilus influenzae purified in DDM
Method: EM (single particle) / Resolution: 3.1 Å

43247

8vi3

EMDB-43247, PDB-8vi3:
TehA from Haemophilus influenzae purified in GDN
Method: EM (single particle) / Resolution: 2.9 Å

43248

8vi4

EMDB-43248, PDB-8vi4:
TehA from Haemophilus influenzae purified in LMNG
Method: EM (single particle) / Resolution: 3.1 Å

43249

8vi5

EMDB-43249, PDB-8vi5:
TehA from Haemophilus influenzae purified in OG
Method: EM (single particle) / Resolution: 3.2 Å

Source
  • haemophilus influenzae (bacteria)
KeywordsMEMBRANE PROTEIN / ANION CHANNEL / ALPHA HELICAL INTEGRAL MEMBRANE PROTEIN

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