The Structural Basis of Ca~(2+) Transport by The Ca~(2+-)ATPase From Skeletal Sarcoplasmic Reticulum
- VernacularTitle:骨骼肌内质网Ca~(2+)泵转运Ca~(2+)的结构基础
- Author:
Risheng WEI
;
Peirong WANG
;
Changcheng YIN
- Publication Type:Journal Article
- Keywords:
Ca2+-pump (Ca2+-ATPase), crystal structure, conformational change
- From:
Progress in Biochemistry and Biophysics
2006;0(03):-
- CountryChina
- Language:Chinese
-
Abstract:
The Ca2+-ATPase of sarcoplasmic reticulum is a Ca2+ pump that plays a key role in regulating cytosol calcium concentration in muscle cells. It undergoes a sequential conformational transition during the transport process. According to the classical E1/E2 theory, in the E1 state the binding sites have high affinity and open to the cytoplasm, whereas in the E2 state the binding sites have low affinity and face the luminal side. Crystal structures of several states during the reaction cycle of Ca2+-ATPase have been solved recently, including a Ca2+-bound form (E1-2Ca2+), a Ca2+-unbound form stabilized by a potent inhibitor thapsigargin (TG) (E2-TG), an ATP-bound form (E1-ATP), an E1-P-ADP state, and an E2-Pi state. The details of these crystal structures and the relationship between structure and function of Ca2+-ATPase during reaction cycle were summarized, and the issues to be addressed in future research were raised.
