期刊
PROTEIN SCIENCE
卷 21, 期 10, 页码 1429-1443出版社
WILEY
DOI: 10.1002/pro.2129
关键词
SERCA; Molecular dynamics; Brownian dynamics; gating; calcium binding
资金
- NSF [OCI-0959097, OCI-1053575]
- National Institutes of Health
- National Science Foundation
- Howard Hughes Medical Institute
- National Biomedical Computation Resource
- Center for Theoretical Biological Physics
- NSF Supercomputer Centers
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.
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