+検索条件
-Structure paper
| タイトル | Cryo-EM reveals transition states of the Acinetobacter baumannii F-ATPase rotary subunits γ and ε, unveiling novel compound targets. |
|---|---|
| ジャーナル・号・ページ | FASEB J, Vol. 38, Issue 20, Page e70131, Year 2024 |
| 掲載日 | 2024年10月28日 |
著者 | Khoa Cong Minh Le / Chui Fann Wong / Volker Müller / Gerhard Grüber / ![]() |
| PubMed 要旨 | Priority 1: critical WHO pathogen Acinetobacter baumannii depends on ATP synthesis and ATP:ADP homeostasis and its bifunctional FF-ATP synthase. While synthesizing ATP, it regulates ATP cleavage by ...Priority 1: critical WHO pathogen Acinetobacter baumannii depends on ATP synthesis and ATP:ADP homeostasis and its bifunctional FF-ATP synthase. While synthesizing ATP, it regulates ATP cleavage by its inhibitory ε subunit to prevent wasteful ATP consumption. We determined cryo-electron microscopy structures of the ATPase active A. baumannii F-αßγε mutant in four distinct conformational states, revealing four transition states and structural transformation of the ε's C-terminal domain, forming the switch of an ATP hydrolysis off- and an ATP synthesis on-state based. These alterations go in concert with altered motions and interactions in the catalytic- and rotary subunits of this engine. These A. baumannii interacting sites provide novel pathogen-specific targets for inhibitors, with the aim of ATP depletion and/or ATP synthesis and growth inhibition. Furthermore, the presented diversity to other bacterial F-ATP synthases extends the view of structural elements regulating such a catalyst. |
リンク | FASEB J / PubMed:39467208 / PubMed Central |
| 手法 | EM (単粒子) |
| 解像度 | 2.89 - 3.18 Å |
| 構造データ | EMDB-60117, PDB-8zi0: EMDB-60118, PDB-8zi1: EMDB-60119, PDB-8zi2: EMDB-60120, PDB-8zi3: |
| 化合物 | ![]() ChemComp-ATP: ![]() ChemComp-MG: ![]() ChemComp-ADP: ![]() ChemComp-PO4: |
| 由来 |
|
キーワード | HYDROLASE / ATP hydrolysis / F1-ATPase |
ムービー
コントローラー
構造ビューア
万見文献について



著者

リンク











acinetobacter baumannii ab5075 (バクテリア)
キーワード