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8VI2

TehA from Haemophilus influenzae purified in DDM

8VI2 の概要
エントリーDOI10.2210/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
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: 38674110
DOI: 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
Validation report summary of 8vi2
検証レポート(詳細版)ダウンロードをダウンロード

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件を2024-11-06に公開中

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