The alternating power stroke of a 6-cylinder AAA protease chaperone engine. Molecular cell [Mol Cell] Journal article

Title	The alternating power stroke of a 6-cylinder AAA protease chaperone engine.
Author(s)	Kress W, Weber-Ban E
Institution	ETH Zurich, Institute of Molecular Biology and Biophysics, Switzerland.
Source	Mol Cell 2009 Sep 11; 35(5):545-7.
MeSH	Adenosine Triphosphatases Adenosine Triphosphate Allosteric Regulation Amino Acid Motifs Binding Sites Catalytic Domain Conserved Sequence Energy Metabolism Fungal Proteins Humans Hydrolysis Kinetics Metalloendopeptidases Mitochondrial Membranes Models, Molecular Molecular Chaperones Protein Subunits Signal Transduction Structure-Activity Relationship Substrate Specificity Yeasts
Abstract	In this issue of Molecular Cell, Augustin et al. (2009) describe the regulatory coupling of adjacent ATP subunits in the mitochondrial AAA protease ring along with the responsible molecular determinants and uncover its importance for membrane dislocation of substrates.
Language	eng
Pub Type(s)	Comment Journal Article
PubMed ID	19748349

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