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Pull-down of Calmodulin-binding Proteins
07:51

Pull-down of Calmodulin-binding Proteins

Published on: January 23, 2012

Calmodulin-induced structural changes in endothelial nitric oxide synthase.

Anthony Persechini1, Quang-Kim Tran, D J Black

  • 1Division of Molecular Biology and Biochemistry and Division of Cell Biology and Biophysics, University of Missouri at Kansas City, 5007 Rockhill Rd, Kansas City, MO 64110-2499, USA. persechinia@umkc.edu

FEBS Letters
|December 26, 2012
PubMed
Summary
This summary is machine-generated.

Calmodulin binding to endothelial nitric oxide synthase (eNOS) repositions reductase domains. This structural change is crucial for eNOS activity and electron transfer, revealing a novel regulatory mechanism.

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09:39

Development and Characterization of In Vitro Microvessel Network and Quantitative Measurements of Endothelial [Ca2+]i and Nitric Oxide Production

Published on: May 19, 2016

Area of Science:

  • Structural Biology
  • Biochemistry
  • Molecular Mechanisms

Background:

  • Endothelial nitric oxide synthase (eNOS) is a critical enzyme regulating vascular tone and function.
  • The precise structural mechanisms governing eNOS activity, particularly the role of calmodulin (CaM) and its reductase domains, remain incompletely understood.

Purpose of the Study:

  • To elucidate the three-dimensional structures of CaM-free and CaM-bound eNOS.
  • To investigate the structural rearrangements induced by CaM binding to eNOS.
  • To propose a model for CaM-mediated regulation of eNOS electron transfer.

Main Methods:

  • Cryo-electron microscopy (cryo-EM) for structural reconstruction.
  • Analysis of electron density maps to model protein domains.

Main Results:

  • CaM-free eNOS structure shows a well-defined oxygenase domain dimer, with mobile and delocalized reductase domains.
  • CaM-bound eNOS reveals additional density near basic patches on the oxygenase domain, indicating CaM and reductase domain interactions.
  • Identified potential docking sites for the reductase domain FMN-binding module and CaM on the oxygenase domain.

Conclusions:

  • CaM binding to eNOS induces significant structural changes, repositioning the reductase domains.
  • CaM binding likely facilitates the docking of reductase domain modules essential for electron transfer.
  • This study proposes a model where CaM acts as a crucial regulator, optimizing eNOS structure for catalytic activity.