6RKE

Molybdenum storage protein - P212121, ADP, molybdate

Summary for 6RKE

• Entry DOI: 10.2210/pdb6rke/pdb
• Descriptor: Molybdenum storage protein subunit beta, (mu3-oxo)-tris(mu2-oxo)-nonakisoxo-trimolybdenum (VI), MO(10)-O(35) Cluster, ... (12 entities in total)
• Functional Keywords: molybdenum storage protein, polyoxomolybdate clusters, atp, amino acid kinase, metal binding protein
• Biological source: Azotobacter vinelandii (strain DJ / ATCC BAA-1303); More
• Total number of polymer chains: 12
• Total formula weight: 373432.31

Authors

Ermler, U.,Bruenle, S. (deposition date: 2019-04-30, release date: 2019-12-18, Last modification date: 2024-01-24)

Primary citation

Brunle, S.,Eisinger, M.L.,Poppe, J.,Mills, D.J.,Langer, J.D.,Vonck, J.,Ermler, U.
Molybdate pumping into the molybdenum storage protein via an ATP-powered piercing mechanism.
Proc.Natl.Acad.Sci.USA, 2019

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 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.

PubMed: 31811022
DOI: 10.1073/pnas.1913031116

Experimental method

X-RAY DIFFRACTION (1.7 Å)