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< | ==Crystal structure of the central axis (NtpD-NtpG) in the catalytic portion of Enterococcus hirae V-type sodium ATPase== | ||
<StructureSection load='3aon' size='340' side='right'caption='[[3aon]], [[Resolution|resolution]] 2.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3aon]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Enterococcus_hirae Enterococcus hirae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AON OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3AON FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> | |||
- | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3aon FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3aon OCA], [https://pdbe.org/3aon PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3aon RCSB], [https://www.ebi.ac.uk/pdbsum/3aon PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3aon ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/NTPD_ENTHA NTPD_ENTHA] Involved in ATP-driven sodium extrusion.<ref>PMID:8157629</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== 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<ref>PMID:22114184</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3aon" style="background-color:#fffaf0;"></div> | |||
== | ==See Also== | ||
[[ | *[[ATPase 3D structures|ATPase 3D structures]] | ||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Enterococcus hirae]] | [[Category: Enterococcus hirae]] | ||
[[Category: Arai | [[Category: Large Structures]] | ||
[[Category: Hossain | [[Category: Arai S]] | ||
[[Category: Ishizuka-Katsura | [[Category: Hossain KMM]] | ||
[[Category: Iwata | [[Category: Ishizuka-Katsura Y]] | ||
[[Category: Kakinuma | [[Category: Iwata S]] | ||
[[Category: Murata | [[Category: Kakinuma Y]] | ||
[[Category: Saijo | [[Category: Murata T]] | ||
[[Category: Shirouzu | [[Category: Saijo S]] | ||
[[Category: Terada | [[Category: Shirouzu M]] | ||
[[Category: Yamato | [[Category: Terada T]] | ||
[[Category: Yokoyama | [[Category: Yamato I]] | ||
[[Category: Yokoyama S]] | |||
Latest revision as of 18:50, 4 October 2023
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
FunctionNTPD_ENTHA Involved in ATP-driven sodium extrusion.[1] Publication Abstract from PubMedV-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. See AlsoReferences
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