2WPD

The Mg.ADP inhibited state of the yeast F1c10 ATP synthase

Summary for 2WPD

• Entry DOI: 10.2210/pdb2wpd/pdb
• Descriptor: ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL, ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL, ATP SYNTHASE SUBUNIT GAMMA, MITOCHONDRIAL, ... (9 entities in total)
• Functional Keywords: atp phosphorylase (h+ transporting), atp-binding, central stalk, hydrolase, atp synthesis, phosphoprotein, membrane protein, lipid-binding, ion transport, nucleotide-binding, hydrogen ion transport
• Biological source: SACCHAROMYCES CEREVISIAE (BAKER'S YEAST); More
• Cellular location: Mitochondrion inner membrane: P07251; Mitochondrion: P00830 P38077 Q12165 P21306; Mitochondrion membrane; Multi-pass membrane protein (Potential): P61829
• Total number of polymer chains: 19
• Total formula weight: 450527.58

Authors

Dautant, A.,Velours, J.,Giraud, M.-F. (deposition date: 2009-08-05, release date: 2010-07-07, Last modification date: 2023-12-20)

Primary citation

Dautant, A.,Velours, J.,Giraud, M.
Crystal Structure of the Mg.Adp-Inhibited State of the Yeast F1C10-ATP Synthase.
J.Biol.Chem., 285:29502-, 2010

PubMed Abstract: The F(1)c(10) subcomplex of the yeast F(1)F(0)-ATP synthase includes the membrane rotor part c(10)-ring linked to a catalytic head, (αβ)(3), by a central stalk, γδε. The Saccharomyces cerevisiae yF(1)c(10)·ADP subcomplex was crystallized in the presence of Mg·ADP, dicyclohexylcarbodiimide (DCCD), and azide. The structure was solved by molecular replacement using a high resolution model of the yeast F(1) and a bacterial c-ring model with 10 copies of the c-subunit. The structure refined to 3.43-Å resolution displays new features compared with the original yF(1)c(10) and with the yF(1) inhibited by adenylyl imidodiphosphate (AMP-PNP) (yF(1)(I-III)). An ADP molecule was bound in both β(DP) and β(TP) catalytic sites. The α(DP)-β(DP) pair is slightly open and resembles the novel conformation identified in yF(1), whereas the α(TP)-β(TP) pair is very closed and resembles more a DP pair. yF(1)c(10)·ADP provides a model of a new Mg·ADP-inhibited state of the yeast F(1). As for the original yF(1) and yF(1)c(10) structures, the foot of the central stalk is rotated by ∼40 ° with respect to bovine structures. The assembly of the F(1) central stalk with the F(0) c-ring rotor is mainly provided by electrostatic interactions. On the rotor ring, the essential cGlu(59) carboxylate group is surrounded by hydrophobic residues and is not involved in hydrogen bonding.

PubMed: 20610387
DOI: 10.1074/JBC.M110.124529

Experimental method

X-RAY DIFFRACTION (3.432 Å)