Insight into the Bind−Lock Mechanism of the Yeast Mitochondrial ATP Synthase Inhibitory Peptide

Biochemistry ◽  
2007 ◽  
Vol 46 (29) ◽  
pp. 8680-8688 ◽  
Author(s):  
Vincent Corvest ◽  
Claude Sigalat ◽  
Francis Haraux
Keyword(s):  
Atp Synthase ◽  
Inhibitory Peptide ◽  
Mitochondrial Atp Synthase ◽  
Insight Into

scholarly journals Structure of a mitochondrial ATP synthase with bound native cardiolipin

eLife ◽  
2019 ◽  
Vol 8 ◽  
Author(s):  
Alexander Mühleip ◽  
Sarah E McComas ◽  
Alexey Amunts
Keyword(s):  
Atp Synthase ◽  
Membrane Curvature ◽  
Dimer Interface ◽  
Functional Roles ◽  
Lipid Interactions ◽  
Mitochondrial Atp Synthase ◽  
Distinct Subunit ◽  
Insight Into ◽  
Membrane Region ◽  
Inhibitory Factor 1

The mitochondrial ATP synthase fuels eukaryotic cells with chemical energy. Here we report the cryo-EM structure of a divergent ATP synthase dimer from mitochondria of Euglena gracilis, a member of the phylum Euglenozoa that also includes human parasites. It features 29 different subunits, 8 of which are newly identified. The membrane region was determined to 2.8 Å resolution, enabling the identification of 37 associated lipids, including 25 cardiolipins, which provides insight into protein-lipid interactions and their functional roles. The rotor-stator interface comprises four membrane-embedded horizontal helices, including a distinct subunit a. The dimer interface is formed entirely by phylum-specific components, and a peripherally associated subcomplex contributes to the membrane curvature. The central and peripheral stalks directly interact with each other. Last, the ATPase inhibitory factor 1 (IF1) binds in a mode that is different from human, but conserved in Trypanosomatids.

scholarly journals The Mitochondrial ATP Synthase: Improved Resolution Cryo-EM Model and Insight into the Structure of the Peripheral Stalk Region

2006 ◽  
Vol 12 (S02) ◽  
pp. 368-369
Author(s):  
J Rubinstein
Keyword(s):  
Atp Synthase ◽  
Peripheral Stalk ◽  
Mitochondrial Atp Synthase ◽  
Insight Into

Extended abstract of a paper presented at Microscopy and Microanalysis 2006 in Chicago, Illinois, USA, July 30 – August 3, 2006

scholarly journals Interactions involved in grasping and locking of the inhibitory peptide IF1 by mitochondrial ATP synthase

2014 ◽  
Vol 1837 (6) ◽  
pp. 761-772 ◽  
Author(s):  
Qian Wu ◽  
Tiona Andrianaivomananjaona ◽  
Emmanuel Tetaud ◽  
Vincent Corvest ◽  
Francis Haraux
Keyword(s):  
Atp Synthase ◽  
Inhibitory Peptide ◽  
Mitochondrial Atp Synthase

scholarly journals The ATP Synthase Deficiency in Human Diseases

Life ◽  
2021 ◽  
Vol 11 (4) ◽  
pp. 325
Author(s):  
Chiara Galber ◽  
Stefania Carissimi ◽  
Alessandra Baracca ◽  
Valentina Giorgio
Keyword(s):  
Oxidative Phosphorylation ◽  
Atp Synthase ◽  
Mitochondrial Protein ◽  
High Energy ◽  
Neurocognitive Disorders ◽  
Human Diseases ◽  
Age Related ◽  
Muscle Tissues ◽  
Mitochondrial Atp Synthase ◽  
Genes Encoding

Human diseases range from gene-associated to gene-non-associated disorders, including age-related diseases, neurodegenerative, neuromuscular, cardiovascular, diabetic diseases, neurocognitive disorders and cancer. Mitochondria participate to the cascades of pathogenic events leading to the onset and progression of these diseases independently of their association to mutations of genes encoding mitochondrial protein. Under physiological conditions, the mitochondrial ATP synthase provides the most energy of the cell via the oxidative phosphorylation. Alterations of oxidative phosphorylation mainly affect the tissues characterized by a high-energy metabolism, such as nervous, cardiac and skeletal muscle tissues. In this review, we focus on human diseases caused by altered expressions of ATP synthase genes of both mitochondrial and nuclear origin. Moreover, we describe the contribution of ATP synthase to the pathophysiological mechanisms of other human diseases such as cardiovascular, neurodegenerative diseases or neurocognitive disorders.

scholarly journals Lysine methylation of mitochondrial ATP synthase subunit c stored in tissues of dogs with hereditary ceroid lipofuscinosis

1994 ◽  
Vol 269 (13) ◽  
pp. 9906-9911
Author(s):  
M.L. Katz ◽  
J.S. Christianson ◽  
N.E. Norbury ◽  
C.L. Gao ◽  
A.N. Siakotos ◽  
...  
Keyword(s):  
Atp Synthase ◽  
Lysine Methylation ◽  
Subunit C ◽  
Ceroid Lipofuscinosis ◽  
Mitochondrial Atp Synthase
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