8VI2
TehA from Haemophilus influenzae purified in DDM
8VI2 の概要
エントリーDOI | 10.2210/pdb8vi2/pdb |
EMDBエントリー | 43246 |
分子名称 | Tellurite resistance protein TehA homolog (1 entity in total) |
機能のキーワード | anion channel, alpha helical integral membrane protein, membrane protein |
由来する生物種 | Haemophilus influenzae |
タンパク質・核酸の鎖数 | 3 |
化学式量合計 | 105757.64 |
構造登録者 | Catalano, C.,Senko, S.,Tran, N.L.,Lucier, K.W.,Farwell, A.C.,Silva, M.S.,Dip, P.V.,Poweleit, N.,Scapin, G. (登録日: 2024-01-03, 公開日: 2024-05-08) |
主引用文献 | 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 Cited by 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: 38674110DOI: 10.3390/ijms25084528 主引用文献が同じPDBエントリー |
実験手法 | ELECTRON MICROSCOPY (3.1 Å) |
構造検証レポート
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