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| ==Cryo-EM structure of the mammalian DP-state ATP synthase FO section== | | ==Cryo-EM structure of the mammalian DP-state ATP synthase FO section== |
| <StructureSection load='6j5a' size='340' side='right'caption='[[6j5a]], [[Resolution|resolution]] 4.35Å' scene=''> | | <SX load='6j5a' size='340' side='right' viewer='molstar' caption='[[6j5a]], [[Resolution|resolution]] 4.35Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[6j5a]] is a 18 chain structure with sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6J5A OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6J5A FirstGlance]. <br> | | <table><tr><td colspan='2'>[[6j5a]] is a 17 chain structure with sequence from [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6J5A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6J5A FirstGlance]. <br> |
| </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</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]] 4.35Å</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=6j5a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6j5a OCA], [http://pdbe.org/6j5a PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6j5a RCSB], [http://www.ebi.ac.uk/pdbsum/6j5a PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6j5a 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=6j5a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6j5a OCA], [https://pdbe.org/6j5a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6j5a RCSB], [https://www.ebi.ac.uk/pdbsum/6j5a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6j5a ProSAT]</span></td></tr> |
| </table> | | </table> |
| == Function == | | == Function == |
| [[http://www.uniprot.org/uniprot/ATP6_PIG ATP6_PIG]] Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. 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. Key component of the proton channel; it may play a direct role in the translocation of protons across the membrane. [[http://www.uniprot.org/uniprot/A0A287B4I0_PIG A0A287B4I0_PIG]] Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. 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.[PIRNR:PIRNR005514] [[http://www.uniprot.org/uniprot/ATP8_PIG ATP8_PIG]] Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. 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. Part of the complex F(0) domain. Minor subunit located with subunit a in the membrane (By similarity). [[http://www.uniprot.org/uniprot/ATPK_PIG ATPK_PIG]] Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. 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. Part of the complex F(0) domain. Minor subunit located with subunit a in the membrane. | | [https://www.uniprot.org/uniprot/A0A286ZYM6_PIG A0A286ZYM6_PIG] |
| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| The mitochondrial adenosine triphosphate (ATP) synthase produces most of the ATP required by mammalian cells. We isolated porcine tetrameric ATP synthase and solved its structure at 6.2-angstrom resolution using a single-particle cryo-electron microscopy method. Two classical V-shaped ATP synthase dimers lie antiparallel to each other to form an H-shaped ATP synthase tetramer, as viewed from the matrix. ATP synthase inhibitory factor subunit 1 (IF1) is a well-known in vivo inhibitor of mammalian ATP synthase at low pH. Two IF1 dimers link two ATP synthase dimers, which is consistent with the ATP synthase tetramer adopting an inhibited state. Within the tetramer, we refined structures of intact ATP synthase in two different rotational conformations at 3.34- and 3.45-A resolution.
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| Cryo-EM structure of the mammalian ATP synthase tetramer bound with inhibitory protein IF1.,Gu J, Zhang L, Zong S, Guo R, Liu T, Yi J, Wang P, Zhuo W, Yang M Science. 2019 Jun 14;364(6445):1068-1075. doi: 10.1126/science.aaw4852. PMID:31197009<ref>PMID:31197009</ref>
| | ==See Also== |
| | | *[[ATPase 3D structures|ATPase 3D structures]] |
| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 6j5a" style="background-color:#fffaf0;"></div>
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| == References == | |
| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </SX> |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
| [[Category: Sus scrofa]] | | [[Category: Sus scrofa]] |
| [[Category: Gu, J]] | | [[Category: Gu J]] |
| [[Category: Yang, M]] | | [[Category: Yang M]] |
| [[Category: Yi, J]] | | [[Category: Yi J]] |
| [[Category: Zhang, L]] | | [[Category: Zhang L]] |
| [[Category: Membrane protein]]
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