EMDB/PDB/SASBDBから引用されている文献のデータベース

キーワード
構造解析手法	All X線回折 NMR 電子顕微鏡小角散乱中性子線回折線維回折粉末回折赤外分光 EPR FRET 理論モデルハイブリッド
著者・登録者
ジャーナル
IF	>30 >20 >10 >5 all

タイトル	ADP-inhibited structure of non-catalytic site-depleted FF-ATPase from thermophilic Bacillus sp. PS-3.
ジャーナル・号・ページ	Biochim Biophys Acta Bioenerg, Vol. 1866, Issue 2, Page 149536, Year 2025
掲載日	2025年4月1日
著者	Ren Kobayashi / Astuki Nakano / Kaoru Mitsuoka / Ken Yokoyama /
PubMed 要旨	The F domain of FF-ATP synthases/ATPases (FF) possesses three catalytic sites on the three αβ interfaces, termed αβ, αβ, and αβ, located mainly on the β subunits. The enzyme also has three ...The F domain of FF-ATP synthases/ATPases (FF) possesses three catalytic sites on the three αβ interfaces, termed αβ, αβ, and αβ, located mainly on the β subunits. The enzyme also has three non-catalytic ATP-binding sites on the three αβ interfaces, located mainly on the α subunits. When ATP does not bind to the non-catalytic site, FF becomes significantly prone to ADP inhibition, ultimately resulting in the loss of ATPase activity. However, the underlying mechanism of ADP inhibition remains unclear. Here, we report the cryo-EM structure of the non-catalytic site-depleted (ΔNC) FF from thermophilic Bacillus sp. PS-3, which completely lacks the ability to bind ATP (and ADP) upon transitioning to the ADP-inhibited form. The structure closely resembled the 81° rotated structure of the wild-type FF, except for minor movements in the C-terminal region of the α subunit. In this structure, unlike the wild-type enzyme, the catalytic site at αβ, responsible for ATP hydrolysis, was occupied by ADP-Mg, with the absence of Pi. Furthermore, the catalytic site at αβ, where ATP enters the F domain during steady-state catalysis, is occupied by ADP, seemingly impeding further ATP binding to the enzyme. The structure suggests that the ADP-inhibited form of the F domain is more likely due to differences in the nucleotide-binding states at the catalytic sites rather than structural differences.
リンク	Biochim Biophys Acta Bioenerg / PubMed:39788275
手法	EM (単粒子)
解像度	2.7 - 5.5 Å
構造データ	EMDB-39165: Non-catalytic site depleted and epsilon C-terminal domain deleted FoF1-ATPase from Bacillus PS3,state1,under ATP saturated condition 手法: EM (単粒子) / 解像度: 3.3 Å EMDB-39174: Non-catalytic site depleted and epsilon C-terminal domain deleted FoF1-ATPase from Bacillus PS3,state2,under ATP saturated condition 手法: EM (単粒子) / 解像度: 3.2 Å EMDB-39175: Non-catalytic site depleted and epsilon C-terminal domain deleted FoF1-ATPase from Bacillus PS3,state3,under ATP saturated condition 手法: EM (単粒子) / 解像度: 3.4 Å EMDB-39178: Non-catalytic site depleted and epsilon C-terminal domain deleted FoF1-ATPase from Bacillus PS3,state1,nucleotide depleted condition 手法: EM (単粒子) / 解像度: 3.8 Å EMDB-39180: Non-catalytic site depleted and epsilon C-terminal domain deleted FoF1-ATPase from Bacillus PS3,state2,nucleotide depleted condition 手法: EM (単粒子) / 解像度: 3.8 Å EMDB-39182: Non-catalytic site depleted and epsilon C-terminal domain deleted FoF1-ATPase from Bacillus PS3,state3,nucleotide depleted condition 手法: EM (単粒子) / 解像度: 5.5 Å 39271 8ygv EMDB-39271, PDB-8ygv: F1 domain of Non-catalytic site depleted and epsilon C-terminal domain deleted FoF1-ATPase from Bacillus PS3,nucleotide depleted condition 手法: EM (単粒子) / 解像度: 3.3 Å 39284 8yh8 EMDB-39284, PDB-8yh8: F1 domain of Non-catalytic site depleted and epsilon C-terminal domain deleted FoF1-ATPase from Bacillus PS3,under ATP saturated condition 手法: EM (単粒子) / 解像度: 2.7 Å
化合物	ChemComp-MG: Unknown entry / マグネシウムジカチオン ChemComp-ADP: ADENOSINE-5'-DIPHOSPHATE / ADP / ADP, エネルギー貯蔵分子YM ChemComp-ATP: ADENOSINE-5'-TRIPHOSPHATE / ATP / ATP, エネルギー貯蔵分子YM
由来	bacillus sp. ps3 (バクテリア)
キーワード	MEMBRANE PROTEIN / Complex / MOTOR PROTEIN