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| | <SX load='6fkh' size='340' side='right' viewer='molstar' caption='[[6fkh]], [[Resolution|resolution]] 4.20Å' scene=''> | | <SX load='6fkh' size='340' side='right' viewer='molstar' caption='[[6fkh]], [[Resolution|resolution]] 4.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6fkh]] 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=6FKH OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6FKH FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6fkh]] 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=6FKH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6FKH 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]] 4.2Å</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=6fkh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6fkh OCA], [http://pdbe.org/6fkh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6fkh RCSB], [http://www.ebi.ac.uk/pdbsum/6fkh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6fkh 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=6fkh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6fkh OCA], [https://pdbe.org/6fkh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6fkh RCSB], [https://www.ebi.ac.uk/pdbsum/6fkh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6fkh ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[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/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/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). [[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/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/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/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/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. | + | [https://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] |
| | <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]]
| + | |
| - | [[Category: Membrane protein]]
| + | |
| - | [[Category: Membrane protein complex]]
| + | |
| - | [[Category: Molecular motor]]
| + | |
| Structural highlights
Function
ATPE_SPIOL Produces ATP from ADP in the presence of a proton gradient across the membrane.[HAMAP-Rule:MF_00530]
Publication Abstract from PubMed
The chloroplast adenosine triphosphate (ATP) synthase uses the electrochemical proton gradient generated by photosynthesis to produce ATP, the energy currency of all cells. Protons conducted through the membrane-embedded Fo motor drive ATP synthesis in the F1 head by rotary catalysis. We determined the high-resolution structure of the complete cF1Fo complex by cryo-electron microscopy, resolving side chains of all 26 protein subunits, the five nucleotides in the F1 head, and the proton pathway to and from the rotor ring. The flexible peripheral stalk redistributes differences in torsional energy across three unequal steps in the rotation cycle. Plant ATP synthase is autoinhibited by a beta-hairpin redox switch in subunit gamma that blocks rotation in the dark.
Structure, mechanism, and regulation of the chloroplast ATP synthase.,Hahn A, Vonck J, Mills DJ, Meier T, Kuhlbrandt W Science. 2018 May 11;360(6389). pii: 360/6389/eaat4318. doi:, 10.1126/science.aat4318. PMID:29748256[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Hahn A, Vonck J, Mills DJ, Meier T, Kuhlbrandt W. Structure, mechanism, and regulation of the chloroplast ATP synthase. Science. 2018 May 11;360(6389). pii: 360/6389/eaat4318. doi:, 10.1126/science.aat4318. PMID:29748256 doi:http://dx.doi.org/10.1126/science.aat4318
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