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| ==Chloroplast F1Fo conformation 1== | | ==Chloroplast F1Fo conformation 1== |
| <SX load='6fkf' size='340' side='right' viewer='molstar' caption='[[6fkf]], [[Resolution|resolution]] 3.10Å' scene=''> | | <SX load='6fkf' size='340' side='right' viewer='molstar' caption='[[6fkf]], [[Resolution|resolution]] 3.15Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[6fkf]] is a 26 chain structure with sequence from [http://en.wikipedia.org/wiki/Spinacia_oleracea Spinacia oleracea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6FKF OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6FKF FirstGlance]. <br> | | <table><tr><td colspan='2'>[[6fkf]] is a 26 chain structure with sequence from [https://en.wikipedia.org/wiki/Spinacia_oleracea Spinacia oleracea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6FKF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6FKF FirstGlance]. <br> |
| </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.15Å</td></tr> |
| <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/H(+)-transporting_two-sector_ATPase H(+)-transporting two-sector ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.14 3.6.3.14] </span></td></tr>
| | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> |
| <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6fkf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6fkf OCA], [http://pdbe.org/6fkf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6fkf RCSB], [http://www.ebi.ac.uk/pdbsum/6fkf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6fkf 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=6fkf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6fkf OCA], [https://pdbe.org/6fkf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6fkf RCSB], [https://www.ebi.ac.uk/pdbsum/6fkf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6fkf ProSAT]</span></td></tr> |
| </table> | | </table> |
| == Function == | | == Function == |
| [[http://www.uniprot.org/uniprot/ATPF_SPIOL ATPF_SPIOL]] 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. Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0). [[http://www.uniprot.org/uniprot/ATPG_SPIOL ATPG_SPIOL]] Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex. [[http://www.uniprot.org/uniprot/ATPI_SPIOL ATPI_SPIOL]] Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. [[http://www.uniprot.org/uniprot/ATPE_SPIOL ATPE_SPIOL]] Produces ATP from ADP in the presence of a proton gradient across the membrane.[HAMAP-Rule:MF_00530] [[http://www.uniprot.org/uniprot/ATPB_SPIOL ATPB_SPIOL]] Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits. [[http://www.uniprot.org/uniprot/ATPH_SPIOL ATPH_SPIOL]] 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.[HAMAP-Rule:MF_01396] Key component of the F(0) channel; it plays a direct role in translocation across the membrane. A homomeric c-ring of 14 subunits forms the central stalk rotor element with the F(1) delta and epsilon subunits.[HAMAP-Rule:MF_01396] [[http://www.uniprot.org/uniprot/ATPA_SPIOL ATPA_SPIOL]] Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. [[http://www.uniprot.org/uniprot/ATPD_SPIOL ATPD_SPIOL]] This protein seems to be part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) into CF(1) or is implicated in proton conduction. [[http://www.uniprot.org/uniprot/ATPX_SPIOL ATPX_SPIOL]] 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). Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0). The b'-subunit is a diverged and duplicated form of b found in plants and photosynthetic bacteria (By similarity). | | [https://www.uniprot.org/uniprot/ATPA_SPIOL ATPA_SPIOL] Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. |
| <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| [[Category: Large Structures]] | | [[Category: Large Structures]] |
| [[Category: Spinacia oleracea]] | | [[Category: Spinacia oleracea]] |
| [[Category: Hahn, A]] | | [[Category: Hahn A]] |
| [[Category: Kuehlbrandt, W]] | | [[Category: Kuehlbrandt W]] |
| [[Category: Meier, T]] | | [[Category: Meier T]] |
| [[Category: Mills, D J]] | | [[Category: Mills DJ]] |
| [[Category: Vonck, J]] | | [[Category: Vonck J]] |
| [[Category: Atp synthase]]
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| [[Category: Membrane protein]]
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| [[Category: Membrane protein complex]]
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| [[Category: Molecular motor]]
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