3aon: Difference between revisions
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3aon FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3aon OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3aon RCSB], [http://www.ebi.ac.uk/pdbsum/3aon PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3aon FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3aon OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3aon RCSB], [http://www.ebi.ac.uk/pdbsum/3aon PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/NTPG_ENTHR NTPG_ENTHR]] Involved in ATP-driven sodium extrusion. | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Enterococcus hirae]] | [[Category: Enterococcus hirae]] | ||
[[Category: Arai, S | [[Category: Arai, S]] | ||
[[Category: Hossain, K M.M | [[Category: Hossain, K M.M]] | ||
[[Category: Ishizuka-Katsura, Y | [[Category: Ishizuka-Katsura, Y]] | ||
[[Category: Iwata, S | [[Category: Iwata, S]] | ||
[[Category: Kakinuma, Y | [[Category: Kakinuma, Y]] | ||
[[Category: Murata, T | [[Category: Murata, T]] | ||
[[Category: Saijo, S | [[Category: Saijo, S]] | ||
[[Category: Shirouzu, M | [[Category: Shirouzu, M]] | ||
[[Category: Terada, T | [[Category: Terada, T]] | ||
[[Category: Yamato, I | [[Category: Yamato, I]] | ||
[[Category: Yokoyama, S | [[Category: Yokoyama, S]] | ||
[[Category: Alpha/beta fold]] | [[Category: Alpha/beta fold]] | ||
[[Category: Central axis]] | [[Category: Central axis]] | ||
Revision as of 14:49, 25 December 2014
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
Function[NTPG_ENTHR] Involved in ATP-driven sodium extrusion. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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