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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

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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]

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