4BEM

Crystal structure of the F-type ATP synthase c-ring from Acetobacterium woodii.

Summary for 4BEM

• Entry DOI: 10.2210/pdb4bem/pdb
• Descriptor: F1FO ATPASE C2 SUBUNIT, F1FO ATPASE C1 SUBUNIT, SODIUM ION, ... (9 entities in total)
• Functional Keywords: hydrolase
• Biological source: ACETOBACTERIUM WOODII; More
• Total number of polymer chains: 10
• Total formula weight: 98896.19

Authors

Matthies, D.,Meier, T.,Yildiz, O. (deposition date: 2013-03-11, release date: 2014-03-26, Last modification date: 2024-10-23)

Primary citation

Matthies, D.,Zhou, W.,Klyszejko, A.L.,Anselmi, C.,Yildiz, O.,Brandt, K.,Muller, V.,Faraldo-Gomez, J.D.,Meier, T.
High-Resolution Structure and Mechanism of an F/V-Hybrid Rotor Ring in a Na+-Coupled ATP Synthase
Nat.Commun., 5:5286-, 2014

PubMed 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.

PubMed: 25381992
DOI: 10.1038/NCOMMS6286

Experimental method

X-RAY DIFFRACTION (2.1 Å)