- EMDB-43248: TehA from Haemophilus influenzae purified in LMNG -
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基本情報
登録情報
データベース: EMDB / ID: EMD-43248
タイトル
TehA from Haemophilus influenzae purified in LMNG
マップデータ
試料
複合体: TELLURITE RESISTANCE PROTEIN TEHA
タンパク質・ペプチド: Tellurite resistance protein TehA homolog
キーワード
ANION CHANNEL / ALPHA HELICAL INTEGRAL MEMBRANE PROTEIN / MEMBRANE PROTEIN
機能・相同性
機能・相同性情報
monoatomic cation efflux transmembrane transporter activity / response to tellurium ion / response to antibiotic / identical protein binding / plasma membrane 類似検索 - 分子機能
Tellurite resistance protein TehA/malic acid transport protein / Tellurite resistance protein TehA / Transporter protein SLAC1/Mae1/ Ssu1/TehA / Voltage-dependent anion channel superfamily / Voltage-dependent anion channel 類似検索 - ドメイン・相同性
Tellurite resistance protein TehA homolog 類似検索 - 構成要素
ジャーナル: Int J Mol Sci / 年: 2024 タイトル: High-Resolution Cryo-Electron Microscopy Structure Determination of Tellurite-Resistance Protein A via 200 kV Transmission Electron Microscopy. 著者: Nhi L Tran / Skerdi Senko / Kyle W Lucier / Ashlyn C Farwell / Sabrina M Silva / Phat V Dip / Nicole Poweleit / Giovanna Scapin / Claudio Catalano / 要旨: 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 ...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.