High-resolution structure and mechanism of an F/V-hybrid rotor ring in a Na+-coupled ATP synthase
Author(s)
Type
Journal Article
Abstract
All rotary ATPases catalyse the interconversion of ATP and ADP-Pi through a mechanism that is coupled to the transmembrane flow of H+ or Na+. Physiologically, however, F/A-type enzymes specialize in ATP synthesis driven by downhill ion diffusion, while eukaryotic V-type ATPases function as ion pumps. To begin to rationalize the molecular basis for this functional differentiation, we solved the crystal structure of the Na+-driven membrane rotor of the Acetobacterium woodii ATP synthase, at 2.1 Å resolution. Unlike known structures, this rotor ring is a 9:1 heteromer of F- and V-type c-subunits and therefore features a hybrid configuration of ion-binding sites along its circumference. Molecular and kinetic simulations are used to dissect the mechanisms of Na+ recognition and rotation of this c-ring, and to explain the functional implications of the V-type c-subunit. These structural and mechanistic insights indicate an evolutionary path between synthases and pumps involving adaptations in the rotor ring.
Date Issued
2014-12
Date Acceptance
2014-09-16
Citation
Nature Communications, 2014, 5 (1), pp.1-14
ISSN
2041-1723
Publisher
Nature Research
Start Page
1
End Page
14
Journal / Book Title
Nature Communications
Volume
5
Issue
1
Copyright Statement
© 2014, Nature Publishing Group, a division of Macmillan Publishers Limited. All Rights Reserved.
Identifier
https://www.nature.com/articles/ncomms6286#Abs1
Subjects
Science & Technology
Multidisciplinary Sciences
Science & Technology - Other Topics
ESSENTIAL ARGININE RESIDUE
C-RING
MOLECULAR ARCHITECTURE
ACETOBACTERIUM-WOODII
PROTON TRANSLOCATION
INTERMEDIATE STEP
H+ TRANSPORT
F-TYPE
SUBUNIT
EVOLUTION
ATP Synthetase Complexes
Acetobacterium
Adenosine Diphosphate
Adenosine Triphosphate
Crystallization
Hydrogen
Microscopy, Atomic Force
Models, Biological
Molecular Dynamics Simulation
Protein Subunits
Sodium
Acetobacterium
Hydrogen
Sodium
ATP Synthetase Complexes
Protein Subunits
Adenosine Diphosphate
Adenosine Triphosphate
Microscopy, Atomic Force
Crystallization
Models, Biological
Molecular Dynamics Simulation
Publication Status
Published
Article Number
5286
Date Publish Online
2014-11-10