ATP-binding Modes and Functionally Important Interdomain Bonds of Sarcoplasmic Reticulum Ca2+-ATPase Revealed by Mutation of Glycine 438, Glutamate 439, and Arginine 678-Reference-Cited by-同舟云学术

ATP-binding Modes and Functionally Important Interdomain Bonds of Sarcoplasmic Reticulum Ca2+-ATPase Revealed by Mutation of Glycine 438, Glutamate 439, and Arginine 678

Published:2007-07 Issue:28 Volume:282 Page:20686-20697
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Clausen Johannes D.,McIntosh David B.,Anthonisen Anne Nyholm,Woolley David G.,Vilsen Bente,Andersen Jens Peter

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference56 articles.

1. Reaction mechanism of Ca2+-dependent ATP hydrolysis by skeletal muscle sarcoplasmic reticulum in the absence of added alkali metal salts. III. Sequential occurrence of ADP-sensitive and ADP-insensitive phosphoenzymes.

2. Energy Interconversion by the Ca2+-Dependent ATPase of the Sarcoplasmic Reticulum

3. Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 Å resolution

4. Structural changes in the calcium pump accompanying the dissociation of calcium

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