5fl7

From Proteopedia

Structure of the F1c10 complex from Yarrowia lipolytica ATP synthase

Structural highlights

5fl7 is a 19 chain structure with sequence from Yarrowia lipolytica. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 3.5Å
Ligands:	ADP, ATP, MG
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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.

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Citations

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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