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	Molybdate pumping into the molybdenum storage protein via an ATP-powered piercing mechanism.
ジャーナル・号・ページ	Proc Natl Acad Sci U S A, Vol. 116, Issue 52, Page 26497-26504, Year 2019
掲載日	2019年12月26日
著者	Steffen Brünle / Martin L Eisinger / Juliane Poppe / Deryck J Mills / Julian D Langer / Janet Vonck / Ulrich Ermler /
PubMed 要旨	The molybdenum storage protein (MoSto) deposits large amounts of molybdenum as polyoxomolybdate clusters in a heterohexameric (αβ) cage-like protein complex under ATP consumption. Here, we suggest ...The molybdenum storage protein (MoSto) deposits large amounts of molybdenum as polyoxomolybdate clusters in a heterohexameric (αβ) cage-like protein complex under ATP consumption. Here, we suggest a unique mechanism for the ATP-powered molybdate pumping process based on X-ray crystallography, cryoelectron microscopy, hydrogen-deuterium exchange mass spectrometry, and mutational studies of MoSto from . First, we show that molybdate, ATP, and Mg consecutively bind into the open ATP-binding groove of the β-subunit, which thereafter becomes tightly locked by fixing the previously disordered N-terminal arm of the α-subunit over the β-ATP. Next, we propose a nucleophilic attack of molybdate onto the γ-phosphate of β-ATP, analogous to the similar reaction of the structurally related UMP kinase. The formed instable phosphoric-molybdic anhydride becomes immediately hydrolyzed and, according to the current data, the released and accelerated molybdate is pressed through the cage wall, presumably by turning aside the Metβ149 side chain. A structural comparison between MoSto and UMP kinase provides valuable insight into how an enzyme is converted into a molecular machine during evolution. The postulated direct conversion of chemical energy into kinetic energy via an activating molybdate kinase and an exothermic pyrophosphatase reaction to overcome a proteinous barrier represents a novelty in ATP-fueled biochemistry, because normally, ATP hydrolysis initiates large-scale conformational changes to drive a distant process.
リンク	Proc Natl Acad Sci U S A / PubMed:31811022 / PubMed Central
手法	EM (単粒子) / X線回折
解像度	1.7 - 3.2 Å
構造データ	4907 6rkd EMDB-4907, PDB-6rkd: Molybdenum storage protein under turnover conditions 手法: EM (単粒子) / 解像度: 3.2 Å PDB-6ris: The Kb42S variant of the molybdenum storage protein 手法: X-RAY DIFFRACTION / 解像度: 2.1 Å PDB-6rj4: Molybdenum storage protein - P6422, ADP 手法: X-RAY DIFFRACTION / 解像度: 1.9 Å PDB-6rke: Molybdenum storage protein - P212121, ADP, molybdate 手法: X-RAY DIFFRACTION / 解像度: 1.7 Å
化合物	ChemComp-ATP: ADENOSINE-5'-TRIPHOSPHATE / ATP / ATP, エネルギー貯蔵分子YM / アデノシン三リン酸 ChemComp-PO4: PHOSPHATE ION / ホスファ-ト / リン酸塩 ChemComp-MG: Unknown entry / マグネシウムジカチオン ChemComp-CL: Unknown entry / クロリド / 塩化物 ChemComp-HOH: WATER / 水 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-NA: Unknown entry / ナトリウムカチオン ChemComp-8M0: bis(mu4-oxo)-tetrakis(mu3-oxo)-hexakis(mu2-oxo)-hexadecaoxo-octamolybdenum (VI) ChemComp-J8E: oxidanyl-[[2,2,4,4,4-pentakis($l^{1}-oxidanyl)-1-(oxidanylmolybdenio)-1$l^{3},3-dioxa-2$l^{5},4$l^{5}-dimolybdacyclobut-2-yl]oxy]molybdenum ChemComp-MOO: MOLYBDATE ION / モリブデン酸塩 ChemComp-OMO: MO(VI)(=O)(OH)2 CLUSTER ChemComp-LJB: MO(8)-O(26) Cluster ChemComp-M10: (mu3-oxo)-tris(mu2-oxo)-nonakisoxo-trimolybdenum (VI) ChemComp-LHW: MO(10)-O(35) Cluster
由来	azotobacter vinelandii dj (窒素固定) azotobacter vinelandii (strain dj / atcc baa-1303) (窒素固定)
キーワード	METAL BINDING PROTEIN / amino acid kinase family / Mo storage (光磁気ディスク) / polyoxomolybdate cluster / ATP hydrolysis / polyoxomolybdate clusters / amino acid kinase / molybdenum storage protein / ATPase (ATPアーゼ) / ATP (アデノシン三リン酸)