Näytä suppeat kuvailutiedot

dc.contributor.authorRaulinaitis, Vytas
dc.contributor.authorTossavainen, Helena
dc.contributor.authorAitio, Olli
dc.contributor.authorJuuti, Jarmo T.
dc.contributor.authorHiramatsu, Keiichi
dc.contributor.authorKontinen, Vesa
dc.contributor.authorPermi, Perttu
dc.date.accessioned2017-08-09T10:57:17Z
dc.date.available2017-08-09T10:57:17Z
dc.date.issued2017
dc.identifier.citationRaulinaitis, V., Tossavainen, H., Aitio, O., Juuti, J. T., Hiramatsu, K., Kontinen, V., & Permi, P. (2017). Identification and structural characterization of LytU, a unique peptidoglycan endopeptidase from the lysostaphin family. <i>Scientific Reports</i>, <i>7</i>, Article 6020. <a href="https://doi.org/10.1038/s41598-017-06135-w" target="_blank">https://doi.org/10.1038/s41598-017-06135-w</a>
dc.identifier.otherCONVID_27136429
dc.identifier.otherTUTKAID_74540
dc.identifier.urihttps://jyx.jyu.fi/handle/123456789/55057
dc.description.abstractWe introduce LytU, a short member of the lysostaphin family of zinc-dependent pentaglycine endopeptidases. It is a potential antimicrobial agent for S. aureus infections and its gene transcription is highly upregulated upon antibiotic treatments along with other genes involved in cell wall synthesis. We found this enzyme to be responsible for the opening of the cell wall peptidoglycan layer during cell divisions in S. aureus. LytU is anchored in the plasma membrane with the active part residing in the periplasmic space. It has a unique Ile/Lys insertion at position 151 that resides in the catalytic site-neighbouring loop and is vital for the enzymatic activity but not affecting the overall structure common to the lysostaphin family. Purified LytU lyses S. aureus cells and cleaves pentaglycine, a reaction conveniently monitored by NMR spectroscopy. Substituting the cofactor zinc ion with a copper or cobalt ion remarkably increases the rate of pentaglycine cleavage. NMR and isothermal titration calorimetry further reveal that, uniquely for its family, LytU is able to bind a second zinc ion which is coordinated by catalytic histidines and is therefore inhibitory. The pH-dependence and high affinity of binding carry further physiological implications.
dc.language.isoeng
dc.publisherNature Publishing Group
dc.relation.ispartofseriesScientific Reports
dc.subject.otherentsyymit
dc.subject.othermetalloproteinaasit
dc.subject.otherantimikrobiset yhdisteet
dc.subject.otherstafylokokit
dc.subject.otherenzymes
dc.subject.othermetalloproteinases
dc.subject.otherantimicrobial compounds
dc.subject.otherstaphylococci
dc.titleIdentification and structural characterization of LytU, a unique peptidoglycan endopeptidase from the lysostaphin family
dc.typearticle
dc.identifier.urnURN:NBN:fi:jyu-201707273366
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.updated2017-07-27T12:15:08Z
dc.type.coarhttp://purl.org/coar/resource_type/c_2df8fbb1
dc.description.reviewstatuspeerReviewed
dc.relation.issn2045-2322
dc.relation.numberinseries0
dc.relation.volume7
dc.type.versionpublishedVersion
dc.rights.copyright© The Author(s) 2017. This is an open access article distributed under the terms of the Creative Commons Attribution License.
dc.rights.accesslevelopenAccessfi
dc.subject.ysoentsyymit
dc.subject.ysometalloproteinaasit
dc.subject.ysoantimikrobiset yhdisteet
dc.subject.ysostafylokokit
jyx.subject.urihttp://www.yso.fi/onto/yso/p4769
jyx.subject.urihttp://www.yso.fi/onto/yso/p23642
jyx.subject.urihttp://www.yso.fi/onto/yso/p21949
jyx.subject.urihttp://www.yso.fi/onto/yso/p18249
dc.rights.urlhttp://creativecommons.org/licenses/by/4.0/
dc.relation.doi10.1038/s41598-017-06135-w
dc.type.okmA1


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Näytä suppeat kuvailutiedot

© The Author(s) 2017. This is an open access article distributed under the terms of the Creative Commons Attribution License.
Ellei muuten mainita, aineiston lisenssi on © The Author(s) 2017. This is an open access article distributed under the terms of the Creative Commons Attribution License.