サブナノメートルの解像度の電子冷凍顕微鏡構造のヘテロジメのABC輸出者の構造
JungMin Kim1, Shenping Wu2, Thomas M Tomasiak2
1Department of Pharmaceutical Chemistry, University of California San Francisco, 600 16th Street, San Francisco, California 94158, USA.
Nature
|November 4, 2014
まとめ
この研究は,TmrAB ABCエクスポーターの構造を内向きの状態で明らかにし,多剤耐性メカニズムに関する洞察を提供します. このトランスポーターを理解する.
科学分野:
- バイオケミストリー バイオケミストリー
- 構造生物学 構造生物学とは
- 分子生物学は分子生物学である.
背景:
- ATP結合カセット (ABC) トランスポーターは,重要な膜タンパク質です.
- ABCの輸出国は,多剤耐性およびヒトの病気に関与しています.
研究 の 目的:
- TmrAB ABCの輸出者の構造を決定する.
- TmrAB.の内向きの形状を明らかにする.
主な方法:
- シングル粒子電子冷凍顕微鏡で,サブナノメートルの解像度.
- 洗剤で溶解したTmrABの構造の決定.
主要な成果:
- TmrAB.の内向きの,ヌクレオチドフリーな形状が解けました.
- トランスメブラン領域でアクセス可能な空洞を特定しました.
- カーボキシ末端ヘリクスを介して,核酸結合ドメインの接触を観察した.
結論:
- TmrAB構造は,内向きのABCトランスポーターのモデルを提供します.
- ニュクレオチド結合ドメインの滑りと回転を含む構成変化メカニズムを示唆する.
- 多剤耐性トランスポーター機能の理解を図る.
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