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dc.contributor.authorCoscia, Francesca
dc.contributor.authorLöwe, Jan
dc.date.accessioned2021-10-18T14:27:08Z
dc.date.available2021-10-18T14:27:08Z
dc.date.issued2021-11
dc.date.submitted2021-08-25
dc.identifier.issn0014-5793
dc.identifier.otherfeb214199
dc.identifier.urihttps://www.repository.cam.ac.uk/handle/1810/329569
dc.description.abstractIn bacteria, Lon is a large hexameric ATP-dependent protease that targets misfolded and also folded substrates, some of which are involved in cell division and survival of cellular stress. The N-terminal domain of Lon facilitates substrate recognition, but how the domains confer such activity has remained unclear. Here, we report the full-length structure of Lon protease from Thermus thermophilus at 3.9 Å resolution in a substrate-engaged state. The six N-terminal domains are arranged in three pairs, stabilized by coiled-coil segments and forming an additional channel for substrate sensing and entry into the AAA+ ring. Sequence conservation analysis and proteolysis assays confirm that this architecture is required for the degradation of both folded and unfolded substrates in bacteria.
dc.languageen
dc.publisherWiley
dc.subjectResearch Letter
dc.subjectResearch Letters
dc.subjectAAA+
dc.subjectcell cycle
dc.subjectcoiled‐coil
dc.subjectLon
dc.subjectprotease
dc.subjectunfolding
dc.titleCryo-EM structure of the full-length Lon protease from Thermus thermophilus.
dc.typeArticle
dc.date.updated2021-10-18T14:27:07Z
prism.publicationNameFEBS Lett
dc.identifier.doi10.17863/CAM.77017
dcterms.dateAccepted2021-09-24
rioxxterms.versionofrecord10.1002/1873-3468.14199
rioxxterms.versionAO
rioxxterms.versionVoR
rioxxterms.licenseref.urihttp://creativecommons.org/licenses/by/4.0/
dc.contributor.orcidCoscia, Francesca [0000-0001-7962-303X]
dc.contributor.orcidLöwe, Jan [0000-0002-5218-6615]
dc.identifier.eissn1873-3468
pubs.funder-project-idMedical Research Council (U105184326)
pubs.funder-project-idWellcome Trust (202754/Z/16/Z)
cam.issuedOnline2021-10-18


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