dc.contributor.authorChaston, Jessica J.
dc.contributor.authorSmits, Callum
dc.contributor.authorAragão, David
dc.contributor.authorWong, Andrew S. W.
dc.contributor.authorAhsan, Bilal
dc.contributor.authorSandin, Sara
dc.contributor.authorMolugu, Sudheer K.
dc.contributor.authorMolugu, Sanjay K.
dc.contributor.authorBernal, Ricardo A.
dc.contributor.authorStock, Daniela
dc.contributor.authorStewart, Alastair G.
dc.date.accessioned2016-04-15T06:39:10Z
dc.date.available2016-04-15T06:39:10Z
dc.date.issued2016
dc.identifier.citationChaston, J., Smits, C., Aragão, D., Wong, A., Ahsan, B., Sandin, S., et al. (2016). Structural and Functional Insights into the Evolution and Stress Adaptation of Type II Chaperonins. Structure, 24(3), 364-374.en_US
dc.identifier.issn0969-2126en_US
dc.identifier.urihttp://hdl.handle.net/10220/40448
dc.description.abstractChaperonins are essential biological complexes assisting protein folding in all kingdoms of life. Whereas homooligomeric bacterial GroEL binds hydrophobic substrates non-specifically, the heterooligomeric eukaryotic CCT binds specifically to distinct classes of substrates. Sulfolobales, which survive in a wide range of temperatures, have evolved three different chaperonin subunits (α, β, γ) that form three distinct complexes tailored for different substrate classes at cold, normal, and elevated temperatures. The larger octadecameric β complexes cater for substrates under heat stress, whereas smaller hexadecameric αβ complexes prevail under normal conditions. The cold-shock complex contains all three subunits, consistent with greater substrate specificity. Structural analysis using crystallography and electron microscopy reveals the geometry of these complexes and shows a novel arrangement of the α and β subunits in the hexadecamer enabling incorporation of the γ subunit.en_US
dc.format.extent39 p.en_US
dc.language.isoenen_US
dc.relation.ispartofseriesStructureen_US
dc.rights© 2016 Elsevier. This is the author created version of a work that has been peer reviewed and accepted for publication by Structure, Elsevier. It incorporates referee’s comments but changes resulting from the publishing process, such as copyediting, structural formatting, may not be reflected in this document. The published version is available at: [http://dx.doi.org/10.1016/j.str.2015.12.016].en_US
dc.subjectBiological Sciences
dc.titleStructural and Functional Insights into the Evolution and Stress Adaptation of Type II Chaperoninsen_US
dc.typeJournal Article
dc.contributor.schoolSchool of Biological Sciencesen_US
dc.identifier.doihttp://dx.doi.org/10.1016/j.str.2015.12.016
dc.description.versionAccepted versionen_US


Files in this item

Thumbnail

This item appears in the following Collection(s)

Show simple item record