5fl7: Difference between revisions
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==Structure of the F1c10 complex from Yarrowia lipolytica ATP synthase== | ==Structure of the F1c10 complex from Yarrowia lipolytica ATP synthase== | ||
<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 [ | <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=' | </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=' | <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'>[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'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [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;"> | |||
== 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<ref>PMID:27373333</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 5fl7" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[ATPase 3D structures|ATPase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Yarrowia lipolytica]] | [[Category: Yarrowia lipolytica]] | ||
[[Category: Bublitz | [[Category: Bublitz M]] | ||
[[Category: Meier | [[Category: Meier T]] | ||
[[Category: Parey | [[Category: Parey K]] | ||
