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dc.contributor.authorKarjalainen, Mikael
dc.contributor.authorHellman, Maarit
dc.contributor.authorTossavainen, Helena
dc.contributor.authorPermi, Perttu
dc.date.accessioned2021-01-27T11:37:13Z
dc.date.available2021-01-27T11:37:13Z
dc.date.issued2021
dc.identifier.citationKarjalainen, M., Hellman, M., Tossavainen, H., & Permi, P. (2021). 1H, 13C, and 15N NMR chemical shift assignment of the complex formed by the first EPEC EspF repeat and N-WASP GTPase binding domain. <i>Biomolecular NMR Assignments</i>, <i>15</i>(1), 213-217. <a href="https://doi.org/10.1007/s12104-021-10008-9" target="_blank">https://doi.org/10.1007/s12104-021-10008-9</a>
dc.identifier.otherCONVID_47830033
dc.identifier.urihttps://jyx.jyu.fi/handle/123456789/73852
dc.description.abstractLEE-encoded effector EspF (EspF) is an effector protein part of enteropathogenic Escherichia coli’s (EPEC’s) arsenal for intestinal infection. This intrinsically disordered protein contains three highly conserved repeats which together compose over half of the protein’s complete amino acid sequence. EPEC uses EspF to hijack host proteins in order to promote infection. In the attack EspF is translocated, together with other effector proteins, to host cell via type III secretion system. Inside host EspF stimulates actin polymerization by interacting with Neural Wiskott-Aldrich syndrome protein (N-WASP), a regulator in actin polymerization machinery. It is presumed that EspF acts by disrupting the autoinhibitory state of N-WASP GTPase binding domain. In this NMR spectroscopy study, we report the 1H, 13C, and 15N resonance assignments for the complex formed by the first 47-residue repeat of EspF and N-WASP GTPase binding domain. These near-complete resonance assignments provide the basis for further studies which aim to characterize structure, interactions, and dynamics between these two proteins in solution.en
dc.format.mimetypeapplication/pdf
dc.languageeng
dc.language.isoeng
dc.publisherSpringer
dc.relation.ispartofseriesBiomolecular NMR Assignments
dc.rightsCC BY 4.0
dc.subject.otherEPEC EspF
dc.subject.otherintrinsically disordered protein
dc.subject.otherN-WASP
dc.subject.otherresonance assignments
dc.subject.othersolution NMR
dc.subject.othertype III secretion system
dc.title1H, 13C, and 15N NMR chemical shift assignment of the complex formed by the first EPEC EspF repeat and N-WASP GTPase binding domain
dc.typearticle
dc.identifier.urnURN:NBN:fi:jyu-202101271313
dc.contributor.laitosKemian laitosfi
dc.contributor.laitosBio- ja ympäristötieteiden laitosfi
dc.contributor.laitosDepartment of Chemistryen
dc.contributor.laitosDepartment of Biological and Environmental Scienceen
dc.contributor.oppiaineFysikaalinen kemiafi
dc.contributor.oppiaineNanoscience Centerfi
dc.contributor.oppiainePhysical Chemistryen
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.format.pagerange213-217
dc.relation.issn1874-2718
dc.relation.numberinseries1
dc.relation.volume15
dc.type.versionpublishedVersion
dc.rights.copyright© Authors, 2021
dc.rights.accesslevelopenAccessfi
dc.relation.grantnumber288235
dc.subject.ysoproteiinit
dc.subject.ysoNMR-spektroskopia
dc.format.contentfulltext
jyx.subject.urihttp://www.yso.fi/onto/yso/p4332
jyx.subject.urihttp://www.yso.fi/onto/yso/p26254
dc.rights.urlhttps://creativecommons.org/licenses/by/4.0/
dc.relation.doi10.1007/s12104-021-10008-9
dc.relation.funderResearch Council of Finlanden
dc.relation.funderSuomen Akatemiafi
jyx.fundingprogramAcademy Project, AoFen
jyx.fundingprogramAkatemiahanke, SAfi
jyx.fundinginformationThis work is supported by the grant from the Academy of Finland (Number 288235 to Perttu Permi). Open Access funding provided by University of Jyväskylä (JYU).
dc.type.okmA1


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