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dc.contributor.authorCzajlik, András
dc.contributor.authorKovács, Bertalan
dc.contributor.authorPermi, Perttu
dc.contributor.authorGáspári, Zoltán
dc.date.accessioned2017-03-31T09:51:02Z
dc.date.available2017-03-31T09:51:02Z
dc.date.issued2017
dc.identifier.citationCzajlik, A., Kovács, B., Permi, P., & Gáspári, Z. (2017). Fine-tuning the extent and dynamics of binding cleft opening as a potential general regulatory mechanism in parvulin-type peptidyl prolyl isomerases. <i>Scientific Reports</i>, <i>7</i>, Article 44504. <a href="https://doi.org/10.1038/srep44504" target="_blank">https://doi.org/10.1038/srep44504</a>
dc.identifier.otherCONVID_26920944
dc.identifier.otherTUTKAID_73337
dc.identifier.urihttps://jyx.jyu.fi/handle/123456789/53429
dc.description.abstractParvulins or rotamases form a distinct group within peptidyl prolyl cis-trans isomerases. Their exact mode of action as well as the role of conserved residues in the family are still not unambiguously resolved. Using backbone S2 order parameters and NOEs as restraints, we have generated dynamic structural ensembles of three distinct parvulins, SaPrsA, TbPin1 and CsPinA. The resulting ensembles are in good agreement with the experimental data but reveal important differences between the three enzymes. The largest difference can be attributed to the extent of the opening of the substrate binding cleft, along which motional mode the three molecules occupy distinct regions. Comparison with a wide range of other available parvulin structures highlights structural divergence along the bottom of the binding cleft acting as a hinge during the opening-closing motion. In the prototype WW-domain containing parvulin, Pin1, this region is also important in forming contacts with the WW domain known to modulate enzymatic activity of the catalytic domain. We hypothesize that modulation of the extent and dynamics of the identified ‘breathing motion’ might be one of the factors responsible for functional differences in the distinct parvulin subfamilies.
dc.language.isoeng
dc.publisherNature Publishing Group
dc.relation.ispartofseriesScientific Reports
dc.subject.otherisomerases
dc.subject.otherparvulins
dc.subject.otherbinding cleft
dc.titleFine-tuning the extent and dynamics of binding cleft opening as a potential general regulatory mechanism in parvulin-type peptidyl prolyl isomerases
dc.typearticle
dc.identifier.urnURN:NBN:fi:jyu-201703241745
dc.contributor.laitosBio- ja ympäristötieteiden laitosfi
dc.contributor.laitosKemian laitosfi
dc.contributor.laitosDepartment of Biological and Environmental Scienceen
dc.contributor.laitosDepartment of Chemistryen
dc.contributor.oppiaineSolu- ja molekyylibiologiafi
dc.contributor.oppiaineOrgaaninen kemiafi
dc.contributor.oppiaineNanoscience Centerfi
dc.contributor.oppiaineCell and Molecular Biologyen
dc.contributor.oppiaineOrganic Chemistryen
dc.contributor.oppiaineNanoscience Centeren
dc.type.urihttp://purl.org/eprint/type/JournalArticle
dc.date.updated2017-03-24T10:15:07Z
dc.type.coarjournal article
dc.description.reviewstatuspeerReviewed
dc.relation.issn2045-2322
dc.relation.numberinseries0
dc.relation.volume7
dc.type.versionpublishedVersion
dc.rights.copyright© the Authors, 2017. This is an open access article distributed under under a Creative Commons Attribution 4.0 International License.
dc.rights.accesslevelopenAccessfi
dc.subject.ysoentsyymit
jyx.subject.urihttp://www.yso.fi/onto/yso/p4769
dc.rights.urlhttps://creativecommons.org/licenses/by/4.0/
dc.relation.doi10.1038/srep44504


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© the Authors, 2017. This is an open access article distributed under under a Creative Commons Attribution 4.0 International License.
Except where otherwise noted, this item's license is described as © the Authors, 2017. This is an open access article distributed under under a Creative Commons Attribution 4.0 International License.