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	Structural Basis of Substrate-Independent Phosphorylation in a P4-ATPase Lipid Flippase.
ジャーナル・号・ページ	J Mol Biol, Vol. 433, Issue 16, Page 167062, Year 2021
掲載日	2021年8月6日
著者	Milena Timcenko / Thibaud Dieudonné / Cédric Montigny / Thomas Boesen / Joseph A Lyons / Guillaume Lenoir / Poul Nissen /
PubMed 要旨	P4-ATPases define a eukaryotic subfamily of the P-type ATPases, and are responsible for the transverse flip of specific lipids from the extracellular or luminal leaflet to the cytosolic leaflet of ...P4-ATPases define a eukaryotic subfamily of the P-type ATPases, and are responsible for the transverse flip of specific lipids from the extracellular or luminal leaflet to the cytosolic leaflet of cell membranes. The enzymatic cycle of P-type ATPases is divided into autophosphorylation and dephosphorylation half-reactions. Unlike most other P-type ATPases, P4-ATPases transport their substrate during dephosphorylation only, i.e. the phosphorylation half-reaction is not associated with transport. To study the structural basis of the distinct mechanisms of P4-ATPases, we have determined cryo-EM structures of Drs2p-Cdc50p from Saccharomyces cerevisiae covering multiple intermediates of the cycle. We identify several structural motifs specific to Drs2p and P4-ATPases in general that decrease movements and flexibility of domains as compared to other P-type ATPases such as Na/K-ATPase or Ca-ATPase. These motifs include the linkers that connect the transmembrane region to the actuator (A) domain, which is responsible for dephosphorylation. Additionally, mutation of Tyr380, which interacts with conserved Asp340 of the distinct DGET dephosphorylation loop of P4-ATPases, highlights a functional role of these P4-ATPase specific motifs in the A-domain. Finally, the transmembrane (TM) domain, responsible for transport, also undergoes less extensive conformational changes, which is ensured both by a longer segment connecting TM helix 4 with the phosphorylation site, and possible stabilization by the auxiliary subunit Cdc50p. Collectively these adaptions in P4-ATPases are responsible for phosphorylation becoming transport-independent.
リンク	J Mol Biol / PubMed:34023399
手法	EM (単粒子)
解像度	2.9 - 3.8 Å
構造データ	12893 7oh4 EMDB-12893: Drs2p-Cdc50p in the E1 state PDB-7oh4: Cryo-EM structure of Drs2p-Cdc50p in the E1 state with PI4P and Mg2+ bound 手法: EM (単粒子) / 解像度: 3.0 Å 12894 7oh5 EMDB-12894: Drs2p-Cdc50p in the E1-AlFx-ADP state PDB-7oh5: Cryo-EM structure of Drs2p-Cdc50p in the E1-AlFx-ADP state 手法: EM (単粒子) / 解像度: 2.9 Å 12895 7oh6 EMDB-12895: Drs2p-Cdc50p in the [PS]E2-AlFx state PDB-7oh6: Cryo-EM structure of Drs2p-Cdc50p in the [PS]E2-AlFx state 手法: EM (単粒子) / 解像度: 3.0 Å 12896 7oh7 EMDB-12896: Drs2p-Cdc50p in the E1-AMPPCP state with PI4P bound PDB-7oh7: Cryo-EM structure of Drs2p-Cdc50p in the E1-AMPPCP state with PI4P bound 手法: EM (単粒子) / 解像度: 3.8 Å
化合物	ChemComp-2Y5: (2R)-1-{[(R)-hydroxy{[(1R,2R,3R,4R,5S,6R)-2,3,5,6-tetrahydroxy-4-(phosphonooxy)cyclohexyl]oxy}phosphoryl]oxy}-3-(octadecanoyloxy)propan-2-yl (5Z,8Z,11Z,14Z)-icosa-5,8,11,14-tetraenoate ChemComp-MG: Unknown entry / マグネシウムジカチオン ChemComp-NAG: 2-acetamido-2-deoxy-beta-D-glucopyranose / N-アセチル-β-D-グルコサミン / N-アセチルグルコサミン ChemComp-HOH: WATER / 水 ChemComp-ALF: TETRAFLUOROALUMINATE ION / テトラフルオロアルミナ-ト ChemComp-ADP: ADENOSINE-5'-DIPHOSPHATE / ADP / ADP, エネルギー貯蔵分子YM / アデノシン二リン酸 ChemComp-Q3G: O-[(R)-[(2S)-2-(hexadecanoyloxy)-3-(octadecanoyloxy)propoxy](hydroxy)phosphoryl]-D-serine / リン脂質YM ChemComp-ACP: PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER / β,γ-メチレンATP / AMP-PCP, エネルギー貯蔵分子類似体*YM
由来	Saccharomyces cerevisiae (パン酵母) saccharomyces cerevisiae (strain atcc 204508 / s288c) (パン酵母)
キーワード	MEMBRANE PROTEIN (膜タンパク質) / Lipid Flippase / P4 ATPase / trans-Golgi Network (ゴルジ体) / Phosphatidylserine transport