caa a22 4500 463208498 CHVBK 20180405153133.0 cr unu---uuuuu 170326e20071201xx s 000 0 eng 10.1007/s10863-007-9106-x doi (NATIONALLICENCE)springer-10.1007/s10863-007-9106-x Roles of transmembrane segment M1 of Na+,K+-ATPase and Ca2+-ATPase, the gatekeeper and the pivot [Elektronische Daten] [Anja Einholm, Jens Andersen, Bente Vilsen] In this review we summarize mutagenesis work on the structure-function relationship of transmembrane segment M1 in the Na+,K+-ATPase and the sarco(endo)plasmic reticulum Ca2+-ATPase. The original hypothesis that charged residues in the N-terminal part of M1 interact with the transported cations can be rejected. On the other hand hydrophobic residues in the middle part of M1 turned out to play crucial roles in Ca2+ interaction/occlusion in Ca2+-ATPase and K+ interaction/occlusion in Na+,K+-ATPase. Leu65 of the Ca2+-ATPase and Leu99 of the Na+,K+-ATPase, located at homologous positions in M1, function as gate-locking residues that restrict the mobility of the side chain of the cation binding/gating residue of transmembrane segment M4, Glu309/Glu329. A pivot formed between a pair of a glycine and a bulky residue in M1 and M3 seems critical to the opening of the extracytoplasmic gate in both the Ca2+-ATPase and the Na+,K+-ATPase. Springer Science+Business Media, LLC, 2007 Na+,K+-ATPase nationallicence Ca2+-ATPase nationallicence Transmembrane segment M1 nationallicence Ion occlusion nationallicence Leucine nationallicence P-type ATPase nationallicence Gating nationallicence Einholm Anja Institute of Physiology and Biophysics, University of Aarhus, Aarhus, Denmark aut Andersen Jens Institute of Physiology and Biophysics, University of Aarhus, Aarhus, Denmark aut Vilsen Bente Institute of Physiology and Biophysics, University of Aarhus, Aarhus, Denmark aut Journal of Bioenergetics and Biomembranes Springer US; http://www.springer-ny.com 39/5-6(2007-12-01), 357-366 0145-479X 39:5-6<357 2007 39 10863 https://doi.org/10.1007/s10863-007-9106-x text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/s10863-007-9106-x text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Einholm Anja Institute of Physiology and Biophysics, University of Aarhus, Aarhus, Denmark aut NATIONALLICENCE 700 1- Andersen Jens Institute of Physiology and Biophysics, University of Aarhus, Aarhus, Denmark aut NATIONALLICENCE 700 1- Vilsen Bente Institute of Physiology and Biophysics, University of Aarhus, Aarhus, Denmark aut NATIONALLICENCE 773 0- Journal of Bioenergetics and Biomembranes Springer US; http://www.springer-ny.com 39/5-6(2007-12-01), 357-366 0145-479X 39:5-6<357 2007 39 10863 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer