Structure and mechanism of Zn2+-transporting P-type ATPases
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چکیده
منابع مشابه
Ion Motive ATPases: V- and P-type ATPases
Biological membranes are composed of phospholipid bilayers and mark the boundaries between the cell or organelle and its exterior. There is little, if any, free diffusion of ions or hydrophilic solutes across phospholipid bilayers. Thus, to enable the cell to control the composition of its intracellular environment, nature has evolved membrane proteins that form specialized pathways across them...
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P-type ATPases are a large family of membrane proteins that perform active ion transport across biological membranes. In these proteins the energy-providing ATP hydrolysis is coupled to ion-transport that builds up or maintains the electrochemical potential gradients of one or two ion species across the membrane. P-type ATPases are found in virtually all eukaryotic cells and also in bacteria, a...
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Copper ATPases, in analogy with other members of the P-ATPase superfamily, contain a catalytic headpiece including an aspartate residue reacting with ATP to form a phosphoenzyme intermediate, and transmembrane helices containing cation-binding sites [TMBS (transmembrane metal-binding sites)] for catalytic activation and cation translocation. Following phosphoenzyme formation by utilization of A...
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Most P-type ATPases pump specific cations or heavy metals across a membrane to form ion gradients. However, the type IV P-type ATPases evolved the ability to transport specific phospholipid substrates rather than cations and function to establish plasma membrane asymmetry in eukaryotic cells. The mechanism for how a P-type ATPase, or any other transporter, can recognize and flip a phospholipid ...
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The copper-transporting P-type ATPases (Cu-ATPases), ATP7A and ATP7B, are essential for the regulation of intracellular copper homeostasis. In this report we describe new roles for glutathione (GSH) and glutaredoxin1 (GRX1) in Cu homeostasis through their regulation of Cu-ATPase activity. GRX1 is a thiol oxidoreductase that catalyzes the reversible reduction of GSH-mixed disulfides to their res...
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ژورنال
عنوان ژورنال: Nature
سال: 2014
ISSN: 0028-0836,1476-4687
DOI: 10.1038/nature13618