3AON: Crystal Structure Of The Central Axis (Ntpd-Ntpg) In The Catalytic Portion Of Enterococcus Hirae V-Type Sodium Atpase

V-ATPases function as ATP-dependent ion pumps in various membrane systems of living organisms. ATP hydrolysis causes rotation of the central rotor complex, which is composed of the central axis D subunit and a membrane c ring that are connected by F and d subunits. Here we determined the crystal structure of the DF complex of the prokaryotic V-ATPase of Enterococcus hirae at 2.0-A resolution. The structure of the D subunit comprised a long left-handed coiled coil with a unique short beta-hairpin region that is effective in stimulating the ATPase activity of V(1)-ATPase by twofold. The F subunit is bound to the middle portion of the D subunit. The C-terminal helix of the F subunit, which was believed to function as a regulatory region by extending into the catalytic A(3)B(3) complex, contributes to tight binding to the D subunit by forming a three-helix bundle. Both D and F subunits are necessary to bind the d subunit that links to the c ring. From these findings, we modeled the entire rotor complex (DFdc ring) of V-ATPase.
PDB ID: 3AONDownload
MMDB ID: 94009
PDB Deposition Date: 2010/10/4
Updated in MMDB: 2011/12
Experimental Method:
x-ray diffraction
Resolution: 2  Å
Source Organism:
Similar Structures:
Biological Unit for 3AON: dimeric; determined by author and by software (PISA)
Molecular Components in 3AON
Label Count Molecule
Proteins (2 molecules)
V-type Sodium Atpase Subunit D
Molecule annotation
V-type Sodium Atpase Subunit G
Molecule annotation
Chemical (1 molecule)
* Click molecule labels to explore molecular sequence information.

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