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| | ==Crystal structure of the sodium binding rotor ring at pH 5.3== | | ==Crystal structure of the sodium binding rotor ring at pH 5.3== |
| - | <StructureSection load='3zk1' size='340' side='right' caption='[[3zk1]], [[Resolution|resolution]] 2.20Å' scene=''> | + | <StructureSection load='3zk1' size='340' side='right'caption='[[3zk1]], [[Resolution|resolution]] 2.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3zk1]] 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=3ZK1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ZK1 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3zk1]] is a 22 chain structure with sequence from [https://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=3ZK1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZK1 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=LMT:DODECYL-BETA-D-MALTOSIDE'>LMT</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=TAM:TRIS(HYDROXYETHYL)AMINOMETHANE'>TAM</scene></td></tr> | + | </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=LMT:DODECYL-BETA-D-MALTOSIDE'>LMT</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=TAM:TRIS(HYDROXYETHYL)AMINOMETHANE'>TAM</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3zk2|3zk2]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3zk2|3zk2]]</div></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=3zk1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zk1 OCA], [http://pdbe.org/3zk1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3zk1 RCSB], [http://www.ebi.ac.uk/pdbsum/3zk1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3zk1 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=3zk1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zk1 OCA], [https://pdbe.org/3zk1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zk1 RCSB], [https://www.ebi.ac.uk/pdbsum/3zk1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zk1 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). |
| | <div style="background-color:#fffaf0;"> | | <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/> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Bacillus fusiformis veillon and zuber 1898]] | | [[Category: Bacillus fusiformis veillon and zuber 1898]] |
| | + | [[Category: Large Structures]] |
| | [[Category: Meier, T]] | | [[Category: Meier, T]] |
| | [[Category: Schulz, S]] | | [[Category: Schulz, S]] |
| Structural highlights
Function
[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).
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Schulz S, Iglesias-Cans M, Krah A, Yildiz O, Leone V, Matthies D, Cook GM, Faraldo-Gomez JD, Meier T. A new type of na(+)-driven ATP synthase membrane rotor with a two-carboxylate ion-coupling motif. PLoS Biol. 2013 Jun;11(6):e1001596. doi: 10.1371/journal.pbio.1001596. Epub 2013 , Jun 25. PMID:23824040 doi:10.1371/journal.pbio.1001596
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