000453195 001__ 453195
000453195 005__ 20250729151034.0
000453195 0247_ $$2doi$$a10.1371/journal.pone.0242677
000453195 0247_ $$2datacite_doi$$a10.3204/PUBDB-2020-05031
000453195 0247_ $$2altmetric$$aaltmetric:95748107
000453195 0247_ $$2pmid$$apmid:33296386
000453195 0247_ $$2WOS$$aWOS:000598626100043
000453195 0247_ $$2openalex$$aopenalex:W3113068668
000453195 037__ $$aPUBDB-2020-05031
000453195 041__ $$aEnglish
000453195 082__ $$a610
000453195 1001_ $$00000-0002-2563-8786$$aSajko, Sara$$b0
000453195 245__ $$aStructures of three MORN repeat proteins and a re-evaluation of the proposed lipid-binding properties of MORN repeats
000453195 260__ $$aSan Francisco, California, US$$bPLOS$$c2020
000453195 3367_ $$2DRIVER$$aarticle
000453195 3367_ $$2DataCite$$aOutput Types/Journal article
000453195 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article$$bjournal$$mjournal$$s1608201155_29652
000453195 3367_ $$2BibTeX$$aARTICLE
000453195 3367_ $$2ORCID$$aJOURNAL_ARTICLE
000453195 3367_ $$00$$2EndNote$$aJournal Article
000453195 520__ $$aMORN (Membrane Occupation and Recognition Nexus) repeat proteins have a wide taxonomic distribution, being found in both prokaryotes and eukaryotes. Despite this ubiquity, they remain poorly characterised at both a structural and a functional level compared to other common repeats. In functional terms, they are often assumed to be lipid-binding modules that mediate membrane targeting. We addressed this putative activity by focusing on a protein composed solely of MORN repeats—Trypanosoma brucei MORN1. Surprisingly, no evidence for binding to membranes or lipid vesicles by TbMORN1 could be obtained either in vivo or in vitro. Conversely, TbMORN1 did interact with individual phospholipids. High- and low-resolution structures of the MORN1 protein from Trypanosoma brucei and homologous proteins from the parasites Toxoplasma gondii and Plasmodium falciparum were obtained using a combination of macromolecular crystallography, small-angle X-ray scattering, and electron microscopy. This enabled a first structure-based definition of the MORN repeat itself. Furthermore, all three structures dimerised via their C-termini in an antiparallel configuration. The dimers could form extended or V-shaped quaternary structures depending on the presence of specific interface residues. This work provides a new perspective on MORN repeats, showing that they are protein-protein interaction modules capable of mediating both dimerisation and oligomerisation. 
000453195 536__ $$0G:(DE-HGF)POF3-6G3$$a6G3 - PETRA III (POF3-622)$$cPOF3-622$$fPOF III$$x0
000453195 588__ $$aDataset connected to CrossRef
000453195 693__ $$0EXP:(DE-H253)P-P12-20150101$$1EXP:(DE-H253)PETRAIII-20150101$$6EXP:(DE-H253)P-P12-20150101$$aPETRA III$$fPETRA Beamline P12$$x0
000453195 7001_ $$aGrishkovskaya, Irina$$b1
000453195 7001_ $$aKostan, Julius$$b2
000453195 7001_ $$aGraewert, Melissa$$b3
000453195 7001_ $$aSetiawan, Kim$$b4
000453195 7001_ $$aTrübestein, Linda$$b5
000453195 7001_ $$aNiedermüller, Korbinian$$b6
000453195 7001_ $$aGehin, Charlotte$$b7
000453195 7001_ $$aSponga, Antonio$$b8
000453195 7001_ $$aPuchinger, Martin$$b9
000453195 7001_ $$aGavin, Anne-Claude$$b10
000453195 7001_ $$aLeonard, Thomas A.$$b11
000453195 7001_ $$0P:(DE-HGF)0$$aSvergun, Dimitri I.$$b12
000453195 7001_ $$aSmith, Terry K.$$b13
000453195 7001_ $$00000-0001-7031-3801$$aMorriswood, Brooke$$b14
000453195 7001_ $$0P:(DE-HGF)0$$aDjinovic-Carugo, Kristina$$b15$$eCorresponding author
000453195 773__ $$0PERI:(DE-600)2267670-3$$a10.1371/journal.pone.0242677$$gVol. 15, no. 12, p. e0242677 -$$n12$$pe0242677 -$$tPLOS ONE$$v15$$x1932-6203$$y2020
000453195 8564_ $$uhttps://journals.plos.org/plosone/article?id=10.1371/journal.pone.0242677
000453195 8564_ $$uhttps://bib-pubdb1.desy.de/record/453195/files/Structures%20of%20three%20MORN%20repeat%20proteins%20and%20a%20re%20evaluation%20of%20the%20proposed%20lipidbinding%20properties%20of%20MORN%20repeats.pdf$$yOpenAccess
000453195 8564_ $$uhttps://bib-pubdb1.desy.de/record/453195/files/Structures%20of%20three%20MORN%20repeat%20proteins%20and%20a%20re%20evaluation%20of%20the%20proposed%20lipidbinding%20properties%20of%20MORN%20repeats.gif?subformat=icon$$xicon$$yOpenAccess
000453195 8564_ $$uhttps://bib-pubdb1.desy.de/record/453195/files/Structures%20of%20three%20MORN%20repeat%20proteins%20and%20a%20re%20evaluation%20of%20the%20proposed%20lipidbinding%20properties%20of%20MORN%20repeats.jpg?subformat=icon-1440$$xicon-1440$$yOpenAccess
000453195 8564_ $$uhttps://bib-pubdb1.desy.de/record/453195/files/Structures%20of%20three%20MORN%20repeat%20proteins%20and%20a%20re%20evaluation%20of%20the%20proposed%20lipidbinding%20properties%20of%20MORN%20repeats.jpg?subformat=icon-180$$xicon-180$$yOpenAccess
000453195 8564_ $$uhttps://bib-pubdb1.desy.de/record/453195/files/Structures%20of%20three%20MORN%20repeat%20proteins%20and%20a%20re%20evaluation%20of%20the%20proposed%20lipidbinding%20properties%20of%20MORN%20repeats.jpg?subformat=icon-640$$xicon-640$$yOpenAccess
000453195 8564_ $$uhttps://bib-pubdb1.desy.de/record/453195/files/Structures%20of%20three%20MORN%20repeat%20proteins%20and%20a%20re%20evaluation%20of%20the%20proposed%20lipidbinding%20properties%20of%20MORN%20repeats.pdf?subformat=pdfa$$xpdfa$$yOpenAccess
000453195 909CO $$ooai:bib-pubdb1.desy.de:453195$$pdnbdelivery$$pdriver$$pVDB$$popen_access$$popenaire
000453195 9101_ $$0I:(DE-588b)235011-7$$6P:(DE-HGF)0$$aEuropean Molecular Biology Laboratory$$b12$$kEMBL
000453195 9131_ $$0G:(DE-HGF)POF3-622$$1G:(DE-HGF)POF3-620$$2G:(DE-HGF)POF3-600$$3G:(DE-HGF)POF3$$4G:(DE-HGF)POF$$9G:(DE-HGF)POF3-6G3$$aDE-HGF$$bForschungsbereich Materie$$lVon Materie zu Materialien und Leben$$vFacility topic: Research on Matter with Brilliant Light Sources$$x0
000453195 9141_ $$y2020
000453195 915__ $$0LIC:(DE-HGF)CCBY4$$2HGFVOC$$aCreative Commons Attribution CC BY 4.0
000453195 915__ $$0StatID:(DE-HGF)0200$$2StatID$$aDBCoverage$$bSCOPUS$$d2020-08-32
000453195 915__ $$0StatID:(DE-HGF)0160$$2StatID$$aDBCoverage$$bEssential Science Indicators$$d2020-08-32
000453195 915__ $$0StatID:(DE-HGF)1050$$2StatID$$aDBCoverage$$bBIOSIS Previews$$d2020-08-32
000453195 915__ $$0StatID:(DE-HGF)1190$$2StatID$$aDBCoverage$$bBiological Abstracts$$d2020-08-32
000453195 915__ $$0StatID:(DE-HGF)0600$$2StatID$$aDBCoverage$$bEbsco Academic Search$$d2020-08-32
000453195 915__ $$0StatID:(DE-HGF)1040$$2StatID$$aDBCoverage$$bZoological Record$$d2020-08-32
000453195 915__ $$0StatID:(DE-HGF)0100$$2StatID$$aJCR$$bPLOS ONE : 2018$$d2020-08-32
000453195 915__ $$0StatID:(DE-HGF)0501$$2StatID$$aDBCoverage$$bDOAJ Seal$$d2020-08-32
000453195 915__ $$0StatID:(DE-HGF)0500$$2StatID$$aDBCoverage$$bDOAJ$$d2020-08-32
000453195 915__ $$0StatID:(DE-HGF)0113$$2StatID$$aWoS$$bScience Citation Index Expanded$$d2020-08-32
000453195 915__ $$0StatID:(DE-HGF)0700$$2StatID$$aFees$$d2020-08-32
000453195 915__ $$0StatID:(DE-HGF)0150$$2StatID$$aDBCoverage$$bWeb of Science Core Collection$$d2020-08-32
000453195 915__ $$0StatID:(DE-HGF)9900$$2StatID$$aIF < 5$$d2020-08-32
000453195 915__ $$0StatID:(DE-HGF)0510$$2StatID$$aOpenAccess
000453195 915__ $$0StatID:(DE-HGF)0030$$2StatID$$aPeer Review$$bASC$$d2020-08-32
000453195 915__ $$0StatID:(DE-HGF)0561$$2StatID$$aArticle Processing Charges$$d2020-08-32
000453195 915__ $$0StatID:(DE-HGF)0300$$2StatID$$aDBCoverage$$bMedline$$d2020-08-32
000453195 915__ $$0StatID:(DE-HGF)0320$$2StatID$$aDBCoverage$$bPubMed Central$$d2020-08-32
000453195 915__ $$0StatID:(DE-HGF)0199$$2StatID$$aDBCoverage$$bClarivate Analytics Master Journal List$$d2020-08-32
000453195 9201_ $$0I:(DE-H253)EMBL-User-20120814$$kEMBL-User$$lEMBL-User$$x0
000453195 9201_ $$0I:(DE-H253)EMBL-20120731$$kEMBL$$lEMBL$$x1
000453195 980__ $$ajournal
000453195 980__ $$aVDB
000453195 980__ $$aUNRESTRICTED
000453195 980__ $$aI:(DE-H253)EMBL-User-20120814
000453195 980__ $$aI:(DE-H253)EMBL-20120731
000453195 9801_ $$aFullTexts