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* Laboratoire Léon Brillouin (CEA-CNRS), 91191 Gif sur Yvette, France; U410 INSERM, Faculté de Médecine Xavier Bichat, 75870 Paris Cédex 18, France; Computational Biology Unit, Bergen Center for Computational Science, University of Bergen, 5008 Bergen, Norway; Laboratoire de Virologie Moléculaire Structurale, 91198 Gif sur Yvette, France; ¶ Skirball Institute, New York University School of Medicine, New York, New York 10012 USA; and || New York Structural Biology Center, New York, New York 10027 USA
Correspondence: Address reprint requests to J.-J. Lacapère, E-mail: lacapere{at}bichat.inserm.fr; or K. Hinsen. E-mail: hinsen{at}llb.saclay.cea.fr.
A method for the flexible docking of high-resolution atomic structures into lower resolution densities derived from electron microscopy is presented. The atomic structure is deformed by an iterative process using combinations of normal modes to obtain the best fit of the electron microscopical density. The quality of the computed structures has been evaluated by several techniques borrowed from crystallography. Two atomic structures of the SERCA1 Ca-ATPase corresponding to different conformations were used as a starting point to fit the electron density corresponding to a different conformation. The fitted models have been compared to published models obtained by rigid domain docking, and their relation to the known crystallographic structures are explored by normal mode analysis. We find that only a few number of modes contribute significantly to the transition. The associated motions involve almost exclusively rotation and translation of the cytoplasmic domains as well as displacement of cytoplasmic loops. We suggest that the movements of the cytoplasmic domains are driven by the conformational change that occurs between nonphosphorylated and phosphorylated intermediate, the latter being mimicked by the presence of vanadate at the phosphorylation site in the electron microscopy structure.
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