Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Molybdate pumping into the molybdenum storage protein via an ATP-powered piercing mechanism.
Journal, issue, pages	Proc Natl Acad Sci U S A, Vol. 116, Issue 52, Page 26497-26504, Year 2019
Publish date	Dec 26, 2019
Authors	Steffen Brünle / Martin L Eisinger / Juliane Poppe / Deryck J Mills / Julian D Langer / Janet Vonck / Ulrich Ermler /
PubMed Abstract	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.
External links	Proc Natl Acad Sci U S A / PubMed:31811022 / PubMed Central
Methods	EM (single particle) / X-ray diffraction
Resolution	1.7 - 3.2 Å
Structure data	4907 6rkd EMDB-4907, PDB-6rkd: Molybdenum storage protein under turnover conditions Method: EM (single particle) / Resolution: 3.2 Å PDB-6ris: The Kb42S variant of the molybdenum storage protein Method: X-RAY DIFFRACTION / Resolution: 2.1 Å PDB-6rj4: Molybdenum storage protein - P6422, ADP Method: X-RAY DIFFRACTION / Resolution: 1.9 Å PDB-6rke: Molybdenum storage protein - P212121, ADP, molybdate Method: X-RAY DIFFRACTION / Resolution: 1.7 Å
Chemicals	ChemComp-ATP: ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying moleculeYM / Adenosine triphosphate ChemComp-PO4: PHOSPHATE ION / Phosphate ChemComp-MG: Unknown entry ChemComp-CL: Unknown entry / Chloride ChemComp-HOH: WATER / Water ChemComp-ADP: ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying moleculeYM / Adenosine diphosphate ChemComp-NA: Unknown entry 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 / Molybdate 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
Source	azotobacter vinelandii dj (bacteria) azotobacter vinelandii (strain dj / atcc baa-1303) (bacteria)
Keywords	METAL BINDING PROTEIN / amino acid kinase family / Mo storage / polyoxomolybdate cluster / ATP hydrolysis / polyoxomolybdate clusters / amino acid kinase / molybdenum storage protein / ATPase / ATP