Rebuilt 3D structure of the chloroplast f1 ATPase-tentoxin complex

The F1 part of the chloroplast H+ adenosine triphosphate (ATP)‐synthase (CF1) strongly interacts with tentoxin, a natural fungous cyclic tetrapeptide known to inhibit the chloroplast enzyme and not the mammalian mitochondrial enzyme. Whereas the synthesis or the hydrolysis of ATP requires the stepwi...

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Veröffentlicht in:	Proteins, structure, function, and bioinformatics structure, function, and bioinformatics, 2002-11, Vol.49 (3), p.302-320
Hauptverfasser:	Minoletti, Claire, Santolini, Jérôme, Haraux, Francis, Pothier, Joël, André, François
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Animals Aspartic Acid - chemistry Bacterial Proton-Translocating ATPases - chemistry Binding Sites Cattle Chloroplast Proton-Translocating ATPases - chemistry Chloroplast Proton-Translocating ATPases - metabolism Crystallography, X-Ray cyclic peptide Enzyme Inhibitors - chemistry Enzyme Inhibitors - metabolism F0F1 ATP synthase homology modeling Imaging, Three-Dimensional local structural alignment Macromolecular Substances Mitochondrial Proton-Translocating ATPases - chemistry Models, Molecular Molecular Sequence Data Motion Nucleotides - metabolism Peptides, Cyclic - chemistry Peptides, Cyclic - metabolism phytotoxin Protein Subunits Rats Sequence Alignment Sequence Homology, Amino Acid spinach chloroplast Spinacia oleracea - enzymology Yeasts - enzymology
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