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| | <StructureSection load='5fl7' size='340' side='right'caption='[[5fl7]], [[Resolution|resolution]] 3.50Å' scene=''> | | <StructureSection load='5fl7' size='340' side='right'caption='[[5fl7]], [[Resolution|resolution]] 3.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5fl7]] is a 19 chain structure with sequence from [http://en.wikipedia.org/wiki/Yarrowia_lipolytica Yarrowia lipolytica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FL7 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5FL7 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5fl7]] is a 19 chain structure with sequence from [https://en.wikipedia.org/wiki/Yarrowia_lipolytica Yarrowia lipolytica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FL7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5FL7 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">X-ray diffraction, [[Resolution|Resolution]] 3.5Å</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> | + | <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='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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5fl7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fl7 OCA], [https://pdbe.org/5fl7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5fl7 RCSB], [https://www.ebi.ac.uk/pdbsum/5fl7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5fl7 ProSAT]</span></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=5fl7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fl7 OCA], [http://pdbe.org/5fl7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5fl7 RCSB], [http://www.ebi.ac.uk/pdbsum/5fl7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5fl7 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/ATP9_YARLI ATP9_YARLI]] 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. A homomeric c-ring of probably 10 subunits is part of the complex rotary element. [[http://www.uniprot.org/uniprot/Q6C326_YARLI Q6C326_YARLI]] Produces ATP from ADP in the presence of a proton gradient across the membrane.[RuleBase:RU003551] [[http://www.uniprot.org/uniprot/Q6CFT7_YARLI Q6CFT7_YARLI]] Produces ATP from ADP in the presence of a proton gradient across the membrane.[RuleBase:RU003553] | + | [https://www.uniprot.org/uniprot/ATPA_YARLI ATPA_YARLI] 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 (PubMed:25759169). F-type ATP synthases 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 (PubMed:27373333). 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 (PubMed:27373333). Subunits alpha/ATP1 and beta/ATP2 form the catalytic core in F(1) (PubMed:27373333). Rotation of the central stalk against the surrounding alpha/ATP1(3)beta/ATP2(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta/ATP2 subunits (PubMed:27373333). Subunit alpha/ATP1 does not bear the catalytic high-affinity ATP-binding sites (PubMed:27373333).<ref>PMID:25759169</ref> <ref>PMID:27373333</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 5fl7" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 5fl7" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[ATPase 3D structures|ATPase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| | [[Category: Yarrowia lipolytica]] | | [[Category: Yarrowia lipolytica]] |
| - | [[Category: Bublitz, M]] | + | [[Category: Bublitz M]] |
| - | [[Category: Meier, T]] | + | [[Category: Meier T]] |
| - | [[Category: Parey, K]] | + | [[Category: Parey K]] |
| - | [[Category: Atp biosynthetic process]]
| + | |
| - | [[Category: Atp synthase family]]
| + | |
| - | [[Category: Atp synthesis/hydrolysis]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Nucleotide binding]]
| + | |
| - | [[Category: Proton transporting]]
| + | |
| - | [[Category: Rotational mechanism]]
| + | |
| Structural highlights
Function
ATPA_YARLI 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 (PubMed:25759169). F-type ATP synthases 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 (PubMed:27373333). 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 (PubMed:27373333). Subunits alpha/ATP1 and beta/ATP2 form the catalytic core in F(1) (PubMed:27373333). Rotation of the central stalk against the surrounding alpha/ATP1(3)beta/ATP2(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta/ATP2 subunits (PubMed:27373333). Subunit alpha/ATP1 does not bear the catalytic high-affinity ATP-binding sites (PubMed:27373333).[1] [2]
Publication Abstract from PubMed
We determined the structure of a complete, dimeric F1Fo-ATP synthase from yeast Yarrowia lipolytica mitochondria by a combination of cryo-EM and X-ray crystallography. The final structure resolves 58 of the 60 dimer subunits. Horizontal helices of subunit a in Fo wrap around the c-ring rotor, and a total of six vertical helices assigned to subunits a, b, f, i, and 8 span the membrane. Subunit 8 (A6L in human) is an evolutionary derivative of the bacterial b subunit. On the lumenal membrane surface, subunit f establishes direct contact between the two monomers. Comparison with a cryo-EM map of the F1Fo monomer identifies subunits e and g at the lateral dimer interface. They do not form dimer contacts but enable dimer formation by inducing a strong membrane curvature of approximately 100 degrees . Our structure explains the structural basis of cristae formation in mitochondria, a landmark signature of eukaryotic cell morphology.
Structure of a Complete ATP Synthase Dimer Reveals the Molecular Basis of Inner Mitochondrial Membrane Morphology.,Hahn A, Parey K, Bublitz M, Mills DJ, Zickermann V, Vonck J, Kuhlbrandt W, Meier T Mol Cell. 2016 Jun 29. pii: S1097-2765(16)30223-4. doi:, 10.1016/j.molcel.2016.05.037. PMID:27373333[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Liu S, Charlesworth TJ, Bason JV, Montgomery MG, Harbour ME, Fearnley IM, Walker JE. The purification and characterization of ATP synthase complexes from the mitochondria of four fungal species. Biochem J. 2015 May 15;468(1):167-75. PMID:25759169 doi:10.1042/BJ20150197
- ↑ Hahn A, Parey K, Bublitz M, Mills DJ, Zickermann V, Vonck J, Kuhlbrandt W, Meier T. Structure of a Complete ATP Synthase Dimer Reveals the Molecular Basis of Inner Mitochondrial Membrane Morphology. Mol Cell. 2016 Jun 29. pii: S1097-2765(16)30223-4. doi:, 10.1016/j.molcel.2016.05.037. PMID:27373333 doi:http://dx.doi.org/10.1016/j.molcel.2016.05.037
- ↑ Hahn A, Parey K, Bublitz M, Mills DJ, Zickermann V, Vonck J, Kuhlbrandt W, Meier T. Structure of a Complete ATP Synthase Dimer Reveals the Molecular Basis of Inner Mitochondrial Membrane Morphology. Mol Cell. 2016 Jun 29. pii: S1097-2765(16)30223-4. doi:, 10.1016/j.molcel.2016.05.037. PMID:27373333 doi:http://dx.doi.org/10.1016/j.molcel.2016.05.037
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