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{{STRUCTURE_3zk2|  PDB=3zk2  |  SCENE=  }}
===Crystal structure of the sodium binding rotor ring at pH 5.3.===


==Function==
==Crystal structure of the sodium binding rotor ring at pH 8.7==
[[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).  
<StructureSection load='3zk2' size='340' side='right'caption='[[3zk2]], [[Resolution|resolution]] 2.63&Aring;' scene=''>
== Structural highlights ==
<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='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='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'>[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>
== Function ==
[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).
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The anaerobic bacterium Fusobacterium nucleatum uses glutamate decarboxylation to generate a transmembrane gradient of Na(+). Here, we demonstrate that this ion-motive force is directly coupled to ATP synthesis, via an F(1)F(0)-ATP synthase with a novel Na(+) recognition motif, shared by other human pathogens. Molecular modeling and free-energy simulations of the rotary element of the enzyme, the c-ring, indicate Na(+) specificity in physiological settings. Consistently, activity measurements showed Na(+) stimulation of the enzyme, either membrane-embedded or isolated, and ATP synthesis was sensitive to the Na(+) ionophore monensin. Furthermore, Na(+) has a protective effect against inhibitors targeting the ion-binding sites, both in the complete ATP synthase and the isolated c-ring. Definitive evidence of Na(+) coupling is provided by two identical crystal structures of the c(1)(1) ring, solved by X-ray crystallography at 2.2 and 2.6 A resolution, at pH 5.3 and 8.7, respectively. Na(+) ions occupy all binding sites, each coordinated by four amino acids and a water molecule. Intriguingly, two carboxylates instead of one mediate ion binding. Simulations and experiments demonstrate that this motif implies that a proton is concurrently bound to all sites, although Na(+) alone drives the rotary mechanism. The structure thus reveals a new mode of ion coupling in ATP synthases and provides a basis for drug-design efforts against this opportunistic pathogen.


==About this Structure==
A new type of na(+)-driven ATP synthase membrane rotor with a two-carboxylate ion-coupling motif.,Schulz S, Iglesias-Cans M, Krah A, Yildiz O, Leone V, Matthies D, Cook GM, Faraldo-Gomez JD, Meier T PLoS Biol. 2013 Jun;11(6):e1001596. doi: 10.1371/journal.pbio.1001596. Epub 2013 , Jun 25. PMID:23824040<ref>PMID:23824040</ref>
[[3zk2]] is a 22 chain structure with sequence from [http://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].
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3zk2" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[ATPase 3D structures|ATPase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Fusobacterium nucleatum]]
[[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"