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==Crystal structure of the sodium binding rotor ring at pH 8.7.==
==Crystal structure of the sodium binding rotor ring at pH 8.7==
<StructureSection load='3zk2' size='340' side='right' caption='[[3zk2]], [[Resolution|resolution]] 2.63&Aring;' scene=''>
<StructureSection load='3zk2' size='340' side='right'caption='[[3zk2]], [[Resolution|resolution]] 2.63&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3zk2]] is a 22 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_fusiformis"_veillon_and_zuber_1898 "bacillus fusiformis" veillon and zuber 1898]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZK2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ZK2 FirstGlance]. <br>
<table><tr><td colspan='2'>[[3zk2]] is a 22 chain structure with sequence from [https://en.wikipedia.org/wiki/Fusobacterium_nucleatum Fusobacterium nucleatum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZK2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZK2 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DMU:DECYL-BETA-D-MALTOPYRANOSIDE'>DMU</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.63&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3zk1|3zk1]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DMU:DECYL-BETA-D-MALTOPYRANOSIDE'>DMU</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></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=3zk2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zk2 OCA], [http://pdbe.org/3zk2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3zk2 RCSB], [http://www.ebi.ac.uk/pdbsum/3zk2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3zk2 ProSAT]</span></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=3zk2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zk2 OCA], [https://pdbe.org/3zk2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zk2 RCSB], [https://www.ebi.ac.uk/pdbsum/3zk2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zk2 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/ATPL_FUSNN ATPL_FUSNN]] F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation (By similarity).  Key component of the F(0) channel; it plays a direct role in translocation across the membrane. A homomeric c-ring of between 10-14 subunits forms the central stalk rotor element with the F(1) delta and epsilon subunits (By similarity).  
[https://www.uniprot.org/uniprot/ATPL_FUSNN ATPL_FUSNN] F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation (By similarity).  Key component of the F(0) channel; it plays a direct role in translocation across the membrane. A homomeric c-ring of between 10-14 subunits forms the central stalk rotor element with the F(1) delta and epsilon subunits (By similarity).
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<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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==See Also==
==See Also==
*[[ATPase|ATPase]]
*[[ATPase 3D structures|ATPase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bacillus fusiformis veillon and zuber 1898]]
[[Category: Fusobacterium nucleatum]]
[[Category: Meier, T]]
[[Category: Large Structures]]
[[Category: Schulz, S]]
[[Category: Meier T]]
[[Category: Yildiz, O]]
[[Category: Schulz S]]
[[Category: Hydrolase]]
[[Category: Yildiz O]]
[[Category: Membrane protein]]
[[Category: Rotor ring]]
Retrieved from "https://proteopedia.org/3zk2"