3AON

Crystal structure of the central axis (NtpD-NtpG) in the catalytic portion of Enterococcus hirae V-type sodium ATPase

Summary for 3AON

• Entry DOI: 10.2210/pdb3aon/pdb
• Descriptor: V-type sodium ATPase subunit D, V-type sodium ATPase subunit G, NITRATE ION, ... (4 entities in total)
• Functional Keywords: v-atpase, enterococcus, coiled-coil, alpha/beta fold, hydrolase, na(+)-atpase, ntpa3-ntpb3, ntpc, central axis
• Biological source: Enterococcus hirae; More
• Total number of polymer chains: 2
• Total formula weight: 38433.13

Authors

Saijo, S.,Arai, S.,Hossain, K.M.M.,Yamato, I.,Kakinuma, Y.,Ishizuka-Katsura, Y.,Terada, T.,Shirouzu, M.,Yokoyama, S.,Iwata, S.,Murata, T. (deposition date: 2010-10-04, release date: 2011-10-05, Last modification date: 2024-10-16)

Primary citation

Saijo, S.,Arai, S.,Hossain, K.M.M.,Yamato, I.,Suzuki, K.,Kakinuma, Y.,Ishizuka-Katsura, Y.,Ohsawa, N.,Terada, T.,Shirouzu, M.,Yokoyama, S.,Iwata, S.,Murata, T.
Crystal structure of the central axis DF complex of the prokaryotic V-ATPase
Proc.Natl.Acad.Sci.USA, 108:19955-19960, 2011

PubMed Abstract: 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-Å resolution. The structure of the D subunit comprised a long left-handed coiled coil with a unique short β-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.

PubMed: 22114184
DOI: 10.1073/pnas.1108810108

Experimental method

X-RAY DIFFRACTION (2 Å)