Unknown

Dataset Information

0

Calcium binding and allosteric signaling mechanisms for the sarcoplasmic reticulum Ca²+ ATPase.

ABSTRACT: The sarcoplasmic reticulum Ca²? ATPase (SERCA) is a membrane-bound pump that utilizes ATP to drive calcium ions from the myocyte cytosol against the higher calcium concentration in the sarcoplasmic reticulum. Conformational transitions associated with Ca²?-binding are important to its catalytic function. We have identified collective motions that partition SERCA crystallographic structures into multiple catalytically-distinct states using principal component analysis. Using Brownian dynamics simulations, we demonstrate the important contribution of surface-exposed, polar residues in the diffusional encounter of Ca²?. Molecular dynamics simulations indicate the role of Glu309 gating in binding Ca²?, as well as subsequent changes in the dynamics of SERCA's cytosolic domains. Together these data provide structural and dynamical insights into a multistep process involving Ca²? binding and catalytic transitions.

SUBMITTER: Kekenes-Huskey PM 

PROVIDER: S-EPMC3526986 | biostudies-literature | 2012 Oct

REPOSITORIES: biostudies-literature

Json Xml
altmetric image

Publications

Calcium binding and allosteric signaling mechanisms for the sarcoplasmic reticulum Ca²+ ATPase.

Kekenes-Huskey Peter M PM   Metzger Vincent T VT   Grant Barry J BJ   Andrew McCammon J J  

Protein science : a publication of the Protein Society 20121001 10

The sarcoplasmic reticulum Ca²⁺ ATPase (SERCA) is a membrane-bound pump that utilizes ATP to drive calcium ions from the myocyte cytosol against the higher calcium concentration in the sarcoplasmic reticulum. Conformational transitions associated with Ca²⁺-binding are important to its catalytic function. We have identified collective motions that partition SERCA crystallographic structures into multiple catalytically-distinct states using principal component analysis. Using Brownian dynamics sim  ...[more]

Similar Datasets

Unknown Binding interactions of porphyrin derivatives with Ca(2+) ATPase of sarcoplasmic reticulum (SERCA1a).
| S-EPMC3670123 | biostudies-literature
Unknown Hofmeister effect of anions on calcium translocation by sarcoplasmic reticulum Ca(2+)-ATPase.
| S-EPMC4593048 | biostudies-other
Unknown Ca2+-ATPase Molecules as a Calcium-Sensitive Membrane-Endoskeleton of Sarcoplasmic Reticulum.
| S-EPMC7961605 | biostudies-literature
Unknown Functional properties of a sarcoplasmic reticulum Ca(2+)-ATPase with an altered Ca(2+)-binding mechanism.
| S-EPMC1135759 | biostudies-other
Unknown Cysteine-674 oxidation and degradation of sarcoplasmic reticulum Ca(2+) ATPase in diabetic pig aorta.
| S-EPMC2654240 | biostudies-literature
Unknown Binding of Ca2+ to the (Ca(2+)-Mg2+)-ATPase of sarcoplasmic reticulum: equilibrium studies.
| S-EPMC1137878 | biostudies-other
Unknown Binding of Ca2+ to the (Ca(2+)-Mg2+)-ATPase of sarcoplasmic reticulum: kinetic studies.
| S-EPMC1137879 | biostudies-other
Unknown Mechanisms of Calcium Leak from Cardiac Sarcoplasmic Reticulum Revealed by Statistical Mechanics.
| S-EPMC6554640 | biostudies-literature
Unknown Mitsugumin 53 attenuates the activity of sarcoplasmic reticulum Ca(2+)-ATPase 1a (SERCA1a) in skeletal muscle.
| S-EPMC3918935 | biostudies-literature
Unknown Ion pathways in the sarcoplasmic reticulum Ca2+-ATPase.
| S-EPMC3624456 | biostudies-literature