Unique Structural and Functional Properties of A1A0 ATPase/Synthase from Archaea
Abstrakt
ATP synthases are present in every life form being the key enzymes of cellular bioenergetics. The enzyme from the Archaea forms a new class of ATPases, A1A0 ATP synthase. This enzyme has unusual structural and functional features, which separate it from F1F0 and V1V0 ATPases as a distinct enzyme class – A1A0 ATPase/synthase. It contains the transmembrane A0 domain and the cytoplasmatic A1 domain, including a specific site for ATP synthesis. The A1 domain is linked to the A0 part by D-subunit, a structural and functional analog of the γ-subunit of F1F0 ATPase. The genomic approach to the study of this enzyme combined with methods of molecular biology, biochemistry and structural biology, will extend the study of A1A0 ATPase/synthase and ATP synthesis to the molecular level.Stahování
Publikováno
15.06.2010
Jak citovat
Vidová, M., & Šmigáň, P. (2010). Unique Structural and Functional Properties of A1A0 ATPase/Synthase from Archaea. Chemické Listy, 104(5). Získáno z http://blog.chemicke-listy.cz/ojs3/index.php/chemicke-listy/article/view/1294
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