By A.G. Lee (Eds.)
Quantity five of Biomembranes covers an enormous team of membrane proteins, the ATPases. The P-type ATPases couple the hydrolysis of ATP to the flow of ions throughout a membrane and are characterised through the formation of a phosphoyrlated intermediate. integrated are the plasma membrane and muscle sarcoplasmic reticulum Ca2+ -ATPases, the (Na+ -K+) -ATPase, the gastric (H+ -K+) -ATPase, the plasma membrane H+ -ATPase of fungi and crops, the Mg2+ - shipping ATPase, the Salmonella typhimurium, and the K+ -ATPase of Escherichia coli, KdpB. the opposite very important sessions of ATPase in eukaryotic platforms are the vacuolar H+ -ATPases and the F0F1 ATP synthase, and, in micro organism, the anion-translocating ATPases, accountable for resistance to arsenicals and antimonials, and the (Na+ -Mg2+) -ATPase of Acholeplasma. ultimately, eukaryotic structures comprise quite a few ectonucleotidases vital, for instance, in hydrolysis of extracellular ATP published as a cotransmitter from cholinergic and adrenergic nerve terminals. quantity five of Biomembranes explores structure-function relationships for those mebrane-bound ATPases.
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S s s 6 L 7 r^ Figure 12. (Continued) F F F F •F Y F Y M Structure of the SR/ER Ca'^-ATPase 19 Immunological studies have been used to clarify the number and arrangement of the transmembrane helices. , 1989). The cytoplasmic location of the N-terminus has also been shown by chemical labeling experiments (Reithmeier and MacLennan, 1981). , 1991) are located on the cytoplasmic side of the membrane, again giving an even number of transmembrane helices. , 1992), corresponding to a luminal location for the M1-M2 loop for the Ca^"^-ATPase of SR.
Toyofuku, T. (1992). Structure-function relationships in the Ca "^ pump of the sarcoplasmic reticulum. Biochem. Soc. Trans. 20, 559-562. , & Varadi, A. (1990). Molecular cloning and chromosomal localization of a sarco/endoplasmic reticulum-type Ca ^-ATPase ofDrosophila melanogaster. Biochem. Biophys. Res. Commun. 173,872-877. , Clarke, D. , Loo, T. , & MacLennan, D. H. (1989). Functional consequences of alterations to amino acids located in the catalytic center (isoleucine 348 to 2+ threonine 357) and nucleotide-binding domain of the Ca -ATPase of sarcoplasmic reticulum.
Biophys. Acta 897, 207-216. , & Baumert, H. G. (1993). Identification of a cross-linked double-peptide from the catalytic site of the Ca "^-ATPase of sarcoplasmic reticulum formed by the Ca ^- and pH-dependent reaction with ATP y-P-imidazolidate. FEBS Lett. 324, 314-318. , & Champeil, P. (1992). The metal sites on sarcoplasmic reticulum membranes that bind lanthanide ions with the highest affinity are not the ATPase Ca transport sites. J. Biol. Chem. 267, 10302-10312. Henderson, I. M. , Khan, M.
ATPases by A.G. Lee (Eds.)