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Tertiary structure and energy coupling in Ca2+-pump system

Authors :
Shamoo, Adil E.
Lockwich, Tim
Cao, Cheng J.
Source :
Molecular and Cellular Biochemistry; December 1990, Vol. 99 Issue: 2 p67-74, 8p
Publication Year :
1990

Abstract

Europium luminescence from europium bound to sarcoplasmic reticulum (Ca<superscript>2+</superscript> Mg<superscript>2+</superscript>)-ATPase indicates that there are two high affinity calcium binding sites. Furthermore, the two calcium ions at the binding sites are highly coordinated by the protein as the number of H<subscript>2</subscript>O molecules surrounding the Ca<superscript>2+</superscript> ions are 3 and 0.5. In the presence of ATP, calcium ions are occluded even further down to 2 and zero H2O molecules, respectively. The Ca<superscript>2+</superscript> - Ca<superscript>2+</superscript> intersite distance is estimated to be 8–9 Å and the average distance from the Ca<superscript>2+</superscript> sites to CrATP is about 18 Å.

Details

Language :
English
ISSN :
03008177 and 15734919
Volume :
99
Issue :
2
Database :
Supplemental Index
Journal :
Molecular and Cellular Biochemistry
Publication Type :
Periodical
Accession number :
ejs15495848
Full Text :
https://doi.org/10.1007/BF00230335