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000008698 0247_ $$2DOI$$a10.1038/nature08701
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000008698 084__ $$2WoS$$aMultidisciplinary Sciences
000008698 1001_ $$0P:(DE-HGF)0$$aZhang, J.$$b0
000008698 245__ $$aMechanism of folding chamber closure in a group II chaperonin
000008698 260__ $$aLondon [u.a.]$$bNature Publising Group$$c2010
000008698 300__ $$a379 - 383
000008698 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article
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000008698 440_0 $$04484$$aNature$$v463$$x0028-0836
000008698 500__ $$aWe acknowledge the support of grants from the National Institutes of Health through the Nanomedicine Development Center Roadmap Initiative, Biomedical Technology Research Center for Structural Biology in National Center for Research Resources, Nanobiology Training Fellowship administered by the Keck Center of the Gulf Coast Consortia and the National Science Foundation.
000008698 520__ $$aGroup II chaperonins are essential mediators of cellular protein folding in eukaryotes and archaea. These oligomeric protein machines, approximately 1 megadalton, consist of two back-to-back rings encompassing a central cavity that accommodates polypeptide substrates. Chaperonin-mediated protein folding is critically dependent on the closure of a built-in lid, which is triggered by ATP hydrolysis. The structural rearrangements and molecular events leading to lid closure are still unknown. Here we report four single particle cryo-electron microscopy (cryo-EM) structures of Mm-cpn, an archaeal group II chaperonin, in the nucleotide-free (open) and nucleotide-induced (closed) states. The 4.3 A resolution of the closed conformation allowed building of the first ever atomic model directly from the single particle cryo-EM density map, in which we were able to visualize the nucleotide and more than 70% of the side chains. The model of the open conformation was obtained by using the deformable elastic network modelling with the 8 A resolution open-state cryo-EM density restraints. Together, the open and closed structures show how local conformational changes triggered by ATP hydrolysis lead to an alteration of intersubunit contacts within and across the rings, ultimately causing a rocking motion that closes the ring. Our analyses show that there is an intricate and unforeseen set of interactions controlling allosteric communication and inter-ring signalling, driving the conformational cycle of group II chaperonins. Beyond this, we anticipate that our methodology of combining single particle cryo-EM and computational modelling will become a powerful tool in the determination of atomic details involved in the dynamic processes of macromolecular machines in solution.
000008698 536__ $$0G:(DE-Juel1)FUEK409$$2G:(DE-HGF)$$aFunktion und Dysfunktion des Nervensystems$$cP33$$x0
000008698 536__ $$0G:(DE-Juel1)FUEK505$$aBioSoft: Makromolekulare Systeme und biologische Informationsverarbeitung$$cP45$$x1
000008698 588__ $$aDataset connected to Web of Science, Pubmed
000008698 650_2 $$2MeSH$$aAdenosine Triphosphate: chemistry
000008698 650_2 $$2MeSH$$aAdenosine Triphosphate: metabolism
000008698 650_2 $$2MeSH$$aAdenosine Triphosphate: pharmacology
000008698 650_2 $$2MeSH$$aAllosteric Regulation
000008698 650_2 $$2MeSH$$aBinding Sites
000008698 650_2 $$2MeSH$$aCryoelectron Microscopy
000008698 650_2 $$2MeSH$$aGroup II Chaperonins: chemistry
000008698 650_2 $$2MeSH$$aGroup II Chaperonins: metabolism
000008698 650_2 $$2MeSH$$aGroup II Chaperonins: ultrastructure
000008698 650_2 $$2MeSH$$aHydrolysis: drug effects
000008698 650_2 $$2MeSH$$aMethanococcus: chemistry
000008698 650_2 $$2MeSH$$aModels, Molecular
000008698 650_2 $$2MeSH$$aProtein Binding
000008698 650_2 $$2MeSH$$aProtein Conformation: drug effects
000008698 650_2 $$2MeSH$$aProtein Folding
000008698 650_2 $$2MeSH$$aProtein Subunits: chemistry
000008698 650_2 $$2MeSH$$aProtein Subunits: metabolism
000008698 650_2 $$2MeSH$$aStructure-Activity Relationship
000008698 650_7 $$00$$2NLM Chemicals$$aProtein Subunits
000008698 650_7 $$056-65-5$$2NLM Chemicals$$aAdenosine Triphosphate
000008698 650_7 $$0EC 3.6.1.-$$2NLM Chemicals$$aGroup II Chaperonins
000008698 650_7 $$2WoSType$$aJ
000008698 7001_ $$0P:(DE-HGF)0$$aBaker, M.L.$$b1
000008698 7001_ $$0P:(DE-Juel1)132018$$aSchröder, G.F.$$b2$$uFZJ
000008698 7001_ $$0P:(DE-HGF)0$$aDouglas, N.R.$$b3
000008698 7001_ $$0P:(DE-HGF)0$$aReissmann, S.$$b4
000008698 7001_ $$0P:(DE-HGF)0$$aJakana, J.$$b5
000008698 7001_ $$0P:(DE-HGF)0$$aDougherty, M.$$b6
000008698 7001_ $$0P:(DE-HGF)0$$aFu, C.J.$$b7
000008698 7001_ $$0P:(DE-HGF)0$$aLevitt, M.$$b8
000008698 7001_ $$0P:(DE-HGF)0$$aLudtke, S.J.$$b9
000008698 7001_ $$0P:(DE-HGF)0$$aFrydman, J.$$b10
000008698 7001_ $$0P:(DE-HGF)0$$aChiu, W.$$b11
000008698 773__ $$0PERI:(DE-600)1413423-8$$a10.1038/nature08701$$gVol. 463, p. 379 - 383$$p379 - 383$$q463<379 - 383$$tNature <London>$$v463$$x0028-0836$$y2010
000008698 8567_ $$2Pubmed Central$$uhttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC2834796
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000008698 9131_ $$0G:(DE-Juel1)FUEK505$$bSchlüsseltechnologien$$kP45$$lBiologische Informationsverarbeitung$$vBioSoft: Makromolekulare Systeme und biologische Informationsverarbeitung$$x1
000008698 9132_ $$0G:(DE-HGF)POF3-551$$1G:(DE-HGF)POF3-550$$2G:(DE-HGF)POF3-500$$aDE-HGF$$bKey Technologies$$lBioSoft  Fundamentals for future Technologies in the fields of Soft Matter and Life Sciences$$vFunctional Macromolecules and Complexes$$x0
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