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dc.contributor.authorNovitskaia, Olga
dc.contributor.authorBuslaev, Pavel
dc.contributor.authorGushchin, Ivan
dc.date.accessioned2020-01-14T08:04:41Z
dc.date.available2020-01-14T08:04:41Z
dc.date.issued2019
dc.identifier.citationNovitskaia, O., Buslaev, P., & Gushchin, I. (2019). Assembly of Spinach Chloroplast ATP Synthase Rotor Ring Protein-Lipid Complex. <i>Frontiers in Molecular Biosciences</i>, <i>6</i>, Article 135. <a href="https://doi.org/10.3389/fmolb.2019.00135" target="_blank">https://doi.org/10.3389/fmolb.2019.00135</a>
dc.identifier.otherCONVID_34003985
dc.identifier.urihttps://jyx.jyu.fi/handle/123456789/67249
dc.description.abstractRotor ATPases are large multisubunit membrane protein complexes found in all kingdoms of life. The membrane parts of these ATPases include a ring-like assembly, so-called c-ring, consisting of several subunits c, plugged by a patch of phospholipids. In this report, we use a nature-inspired approach to model the assembly of the spinach (Spinacia oleracea) c14 ring protein-lipid complex, where partially assembled oligomers are pulled toward each other using a biasing potential. The resulting assemblies contain 23 to 26 encapsulated plug lipids, general position of which corresponds well to experimental maps. However, best fit to experimental data is achieved with 15 to 17 lipids inside the c-ring. In all of the simulations, the lipids from one leaflet (loop side of the c subunit) are ordered and static, whereas the lipids from the other leaflet are disordered and dynamic. Spontaneous permeation of water molecules toward Glu61 at the active site is also observed. The presented assembly approach is expected to be generalizable to other protein complexes with encapsulated lipid patches.en
dc.format.mimetypeapplication/pdf
dc.languageeng
dc.language.isoeng
dc.publisherFrontiers Media
dc.relation.ispartofseriesFrontiers in Molecular Biosciences
dc.rightsCC BY 4.0
dc.subject.othermembrane protein
dc.subject.othermembrane insertion
dc.subject.othercomplex assembly
dc.subject.otherannular lipids
dc.subject.otherprotein-lipid interactions
dc.titleAssembly of Spinach Chloroplast ATP Synthase Rotor Ring Protein-Lipid Complex
dc.typearticle
dc.identifier.urnURN:NBN:fi:jyu-202001141201
dc.contributor.laitosKemian laitosfi
dc.contributor.laitosDepartment of Chemistryen
dc.contributor.oppiaineNanoscience Centerfi
dc.contributor.oppiaineNanoscience Centeren
dc.type.urihttp://purl.org/eprint/type/JournalArticle
dc.type.coarhttp://purl.org/coar/resource_type/c_2df8fbb1
dc.description.reviewstatuspeerReviewed
dc.relation.issn2296-889X
dc.relation.volume6
dc.type.versionpublishedVersion
dc.rights.copyright© 2019 Novitskaia, Buslaev and Gushchin
dc.rights.accesslevelopenAccessfi
dc.subject.ysolipidit
dc.subject.ysoproteiinit
dc.subject.ysoadenosiinitrifosfaatti
dc.subject.ysosolukalvot
dc.format.contentfulltext
jyx.subject.urihttp://www.yso.fi/onto/yso/p4799
jyx.subject.urihttp://www.yso.fi/onto/yso/p4332
jyx.subject.urihttp://www.yso.fi/onto/yso/p13021
jyx.subject.urihttp://www.yso.fi/onto/yso/p2410
dc.rights.urlhttps://creativecommons.org/licenses/by/4.0/
dc.relation.doi10.3389/fmolb.2019.00135
jyx.fundinginformationThis study was funded by the Russian Foundation for Basic Research according to the research project No. 18-34-00986. We are grateful to the Center for Scientific Computing (CSC-IT Center for Science, Espoo, Finland) for computational resources.
dc.type.okmA1


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