5fl7: Difference between revisions
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== 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] | [[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] | ||
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== 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> | |||
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== References == | |||
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