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Conservation of knotted and slipknotted topology in transmembrane transporters

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dc.abstract.enThe existence of nontrivial topology is well accepted in globular proteins but not in membrane proteins. Our comprehensive topological analysis of the Protein Data Bank structures reveals 18 families of transmembrane proteins with nontrivial topology, showing that they constitute a significant number of membrane proteins. Moreover, we found that they comprise one of the largest groups of secondary active transporters. We classified them based on their knotted fingerprint into four groups: three slipknotted and one knotted. Unexpectedly, we found that the same protein can possess two distinct slipknot motifs that correspond to its outward- and inward-open conformational state. Based on the analysis of structures and knotted fingerprints, we show that slipknot topology is directly involved in the conformational transition and substrate transfer. Therefore, entanglement can be used to classify proteins and to find their structure-function relationship. Furthermore, based on the topological analysis of the transmembrane protein structures predicted by AlphaFold, we identified new potentially slipknotted protein families.
dc.affiliationUniwersytet Warszawski
dc.affiliation.departmentWydział Matematyki, Informatyki i Mechaniki
dc.affiliation.otherCentrum Nowych Technologii
dc.contributor.authorZayats, Vasilina
dc.contributor.authorSikora, Maciej
dc.contributor.authorPerlińska, Agata Paulina
dc.contributor.authorStasiulewicz, Adam
dc.contributor.authorGreń, Bartosz
dc.contributor.authorSułkowska, Joanna Ida
dc.date.accessioned2024-10-29T07:20:04Z
dc.date.available2024-10-29T07:20:04Z
dc.date.issued2023-12-05
dc.description.grantnumber#UMO-2018/31/B/NZ1/04016
dc.description.grantnumber#2021/43/I/NZ1/03341
dc.description.grantnumber#2057
dc.description.grantnumber#0003/ID3/2016/64
dc.description.granttitleNational Science Centre
dc.description.granttitleNational Science Centre
dc.description.granttitleEMBO Installation Grant
dc.description.granttitleMNiSW Grant
dc.description.number23
dc.description.versionfinal_author
dc.description.volume122
dc.identifier.doi10.1016/j.bpj.2023.10.031
dc.identifier.eissn1542-0086
dc.identifier.issn0006-3495
dc.identifier.orcid0000-0002-9355-8171
dc.identifier.orcid0009-0003-0289-276X
dc.identifier.orcid0000-0003-2806-1190
dc.identifier.orcid0000-0003-3346-5579
dc.identifier.orcid0000-0001-9971-6807
dc.identifier.orcid0000-0003-2452-0724
dc.identifier.urihttps://repozytorium.uw.edu.pl//handle/item/160567
dc.languageen
dc.pbn.affiliationbiological sciences
dc.relation.ispartofBiophysical Journal
dc.relation.pages4528-4541
dc.rightsCC-BY
dc.sciencecloudsend
dc.share.typeOPEN_REPOSITORY
dc.subject.enKnots in proteins
dc.subject.enSlipknots in proteins
dc.titleConservation of knotted and slipknotted topology in transmembrane transporters
dc.typeJournalArticle
dspace.entity.typePublication