3aon

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

Structural highlights

3aon is a 2 chain structure with sequence from Enterococcus hirae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2Å
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

NTPD_ENTHA Involved in ATP-driven sodium extrusion.^[1]

Publication Abstract from PubMed

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.

Crystal structure of the central axis DF complex of the prokaryotic V-ATPase.,Saijo S, Arai S, Hossain KM, Yamato I, Suzuki K, Kakinuma Y, Ishizuka-Katsura Y, Ohsawa N, Terada T, Shirouzu M, Yokoyama S, Iwata S, Murata T Proc Natl Acad Sci U S A. 2011 Dec 13;108(50):19955-60. Epub 2011 Nov 23. PMID:22114184^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Takase K, Kakinuma S, Yamato I, Konishi K, Igarashi K, Kakinuma Y. Sequencing and characterization of the ntp gene cluster for vacuolar-type Na(+)-translocating ATPase of Enterococcus hirae. J Biol Chem. 1994 Apr 15;269(15):11037-44. PMID:8157629
↑ Saijo S, Arai S, Hossain KM, 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 U S A. 2011 Dec 13;108(50):19955-60. Epub 2011 Nov 23. PMID:22114184 doi:10.1073/pnas.1108810108

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OCA

[1] Takase K, Kakinuma S, Yamato I, Konishi K, Igarashi K, Kakinuma Y. Sequencing and characterization of the ntp gene cluster for vacuolar-type Na(+)-translocating ATPase of Enterococcus hirae. J Biol Chem. 1994 Apr 15;269(15):11037-44. PMID:8157629

[2] Saijo S, Arai S, Hossain KM, 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 U S A. 2011 Dec 13;108(50):19955-60. Epub 2011 Nov 23. PMID:22114184 doi:10.1073/pnas.1108810108

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