Molecular aspects of higher plant P-type Ca2+-ATPases
نویسندگان
چکیده
منابع مشابه
Evolution of Plant P-Type ATPases
Five organisms having completely sequenced genomes and belonging to all major branches of green plants (Viridiplantae) were analyzed with respect to their content of P-type ATPases encoding genes. These were the chlorophytes Ostreococcus tauri and Chlamydomonas reinhardtii, and the streptophytes Physcomitrella patens (a non-vascular moss), Selaginella moellendorffii (a primitive vascular plant)...
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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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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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In the poster that accompanied this article the centre panel, entitled 'Structural and functional features' contains the sub-panel 'Energy coupling' in which the bottom structure should not be labelled 'E1P open' but 'E2P open'.
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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 of one or two ion species across the respective membrane. The pump function of the investigated pumps is described by a so-called Post-Albers cycle. Main features of the pumping process are (1) a ...
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ژورنال
عنوان ژورنال: Biochimica et Biophysica Acta (BBA) - Biomembranes
سال: 2000
ISSN: 0005-2736
DOI: 10.1016/s0005-2736(00)00131-0