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An evolutionarily conserved glycine-tyrosine motif forms a folding core in outer membrane proteins.

dc.contributor.authorMichalik, Marcin
dc.contributor.authorOrwick-Rydmark, Marcella
dc.contributor.authorHabeck, Michael
dc.contributor.authorAlva, Vikram
dc.contributor.authorArnold, Thomas
dc.contributor.authorLinke, Dirk
dc.date.accessioned2017-12-11T14:01:36Z
dc.date.available2017-12-11T14:01:36Z
dc.date.issued2017
dc.relation.ISSN1932-6203
dc.identifier.urihttp://resolver.sub.uni-goettingen.de/purl?gs-1/14931
dc.description.abstractAn intimate interaction between a pair of amino acids, a tyrosine and glycine on neighboring β-strands, has been previously reported to be important for the structural stability of autotransporters. Here, we show that the conservation of this interacting pair extends to nearly all major families of outer membrane β-barrel proteins, which are thought to have originated through duplication events involving an ancestral ββ hairpin. We analyzed the function of this motif using the prototypical outer membrane protein OmpX. Stopped-flow fluorescence shows that two folding processes occur in the millisecond time regime, the rates of which are reduced in the tyrosine mutant. Folding assays further demonstrate a reduction in the yield of folded protein for the mutant compared to the wild-type, as well as a reduction in thermal stability. Taken together, our data support the idea of an evolutionarily conserved 'folding core' that affects the folding, membrane insertion, and thermal stability of outer membrane protein β-barrels.
dc.languageeng
dc.language.isoeng
dc.rightsopenAccess
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/
dc.subjectOuter membrane proteins; Sequence motif analysis; Protein structure; Urea; Tyrosine; Detergents; Sequence alignment; Protein structure comparison
dc.subject.ddc510
dc.subject.meshAmino Acid Motifs
dc.subject.meshAmino Acid Sequence
dc.subject.meshBacterial Outer Membrane Proteins
dc.subject.meshEscherichia coli
dc.subject.meshEscherichia coli Proteins
dc.subject.meshEvolution, Molecular
dc.subject.meshGlycine
dc.subject.meshLipid Bilayers
dc.subject.meshModels, Molecular
dc.subject.meshProtein Folding
dc.subject.meshProtein Structure, Secondary
dc.subject.meshSequence Alignment
dc.subject.meshTyrosine
dc.titleAn evolutionarily conserved glycine-tyrosine motif forms a folding core in outer membrane proteins.
dc.typejournalArticle
dc.identifier.doi10.1371/journal.pone.0182016
dc.type.versionpublishedVersion
dc.bibliographicCitation.volume12
dc.bibliographicCitation.issue8
dc.type.subtypejournalArticle
dc.identifier.pmid28771529
dc.bibliographicCitation.articlenumbere0182016
dc.description.statuspeerReviewed
dc.bibliographicCitation.journalPloS one


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