4XD7

Structure of thermophilic F1-ATPase inhibited by epsilon subunit

Summary for 4XD7

• Entry DOI: 10.2210/pdb4xd7/pdb
• Descriptor: ATP synthase subunit alpha, ATP synthase subunit beta, ATP synthase gamma chain, ... (6 entities in total)
• Functional Keywords: f1-atpase, atp synthase, rotary motor protein, rotational catalysis, bacillus ps3, thermophilic, hydrolase
• Biological source: Bacillus sp. PS3; More
• Cellular location: Cell membrane ; Peripheral membrane protein : Q5KUJ1 Q5KUJ3 Q5KUJ2 Q5KUJ4
• Total number of polymer chains: 8
• Total formula weight: 375685.05

Authors

SHIRAKIHARA, Y.,SHIRATORI, A.,TANIKAWA, H.,NAKASAKO, M.,YOSHIDA, M.,SUZUKI, T. (deposition date: 2014-12-19, release date: 2015-08-26, Last modification date: 2023-11-15)

Primary citation

Shirakihara, Y.,Shiratori, A.,Tanikawa, H.,Nakasako, M.,Yoshida, M.,Suzuki, T.
Structure of a thermophilic F1 -ATPase inhibited by an epsilon-subunit: deeper insight into the epsilon-inhibition mechanism.
Febs J., 282:2895-2913, 2015

PubMed Abstract: F1-ATPase (F1) is the catalytic sector in F(o)F1-ATP synthase that is responsible for ATP production in living cells. In catalysis, its three catalytic β-subunits undergo nucleotide occupancy-dependent and concerted open-close conformational changes that are accompanied by rotation of the γ-subunit. Bacterial and chloroplast F1 are inhibited by their own ε-subunit. In the ε-inhibited Escherichia coli F1 structure, the ε-subunit stabilizes the overall conformation (half-closed, closed, open) of the β-subunits by inserting its C-terminal helix into the α3β3 cavity. The structure of ε-inhibited thermophilic F1 is similar to that of E. coli F1, showing a similar conformation of the ε-subunit, but the thermophilic ε-subunit stabilizes another unique overall conformation (open, closed, open) of the β-subunits. The ε-C-terminal helix 2 and hook are conserved between the two structures in interactions with target residues and in their positions. Rest of the ε-C-terminal domains are in quite different conformations and positions, and have different modes of interaction with targets. This region is thought to serve ε-inhibition differently. For inhibition, the ε-subunit contacts the second catches of some of the β- and α-subunits, the N- and C-terminal helices, and some of the Rossmann fold segments. Those contacts, as a whole, lead to positioning of those β- and α- second catches in ε-inhibition-specific positions, and prevent rotation of the γ-subunit. Some of the structural features are observed even in IF1 inhibition in mitochondrial F1.

PubMed: 26032434
DOI: 10.1111/febs.13329

Experimental method

X-RAY DIFFRACTION (3.9 Å)