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Crystal structure of the N-terminal domain of the trypanosome flagellar protein BILBO1 reveals a ubiquitin fold with a long structured loop for protein binding

dc.rights.licenseopenen_US
dc.contributor.authorVIDILASERIS, Keni
hal.structure.identifierMicrobiologie Fondamentale et Pathogénicité [MFP]
dc.contributor.authorLANDREIN, Nicolas
dc.contributor.authorPIVOVAROVA, Yulia
dc.contributor.authorLESIGANG, Johannes
dc.contributor.authorAEKSIRI, Niran
hal.structure.identifierMicrobiologie Fondamentale et Pathogénicité [MFP]
dc.contributor.authorROBINSON, Derrick
hal.structure.identifierMicrobiologie Fondamentale et Pathogénicité [MFP]
dc.contributor.authorBONHIVERS, Melanie
dc.contributor.authorDONG, Gang
dc.date.accessioned2023-05-31T15:18:47Z
dc.date.available2023-05-31T15:18:47Z
dc.date.issued2020
dc.identifier.issn0021-9258en_US
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/182399
dc.description.abstractEnTrypanosoma brucei is a protist parasite causing sleeping sickness and nagana in sub-Saharan Africa. T. brucei has a single flagellum whose base contains a bulblike invagination of the plasma membrane called the flagellar pocket (FP). Around the neck of the FP on its cytoplasmic face is a structure called the flagellar pocket collar (FPC), which is essential for FP biogenesis. BILBO1 was the first characterized component of the FPC in trypanosomes. BILBO1's N-terminal domain (NTD) plays an essential role in T. brucei FPC biogenesis and is thus vital for the parasite's survival. Here, we report a 1.6-Å resolution crystal structure of TbBILBO1-NTD, which revealed a conserved horseshoe-like hydrophobic pocket formed by an unusually long loop. Results from mutagenesis experiments suggested that another FPC protein, FPC4, interacts with TbBILBO1 by mainly contacting its three conserved aromatic residues Trp-71, Tyr-87, and Phe-89 at the center of this pocket. Our findings disclose the binding site of TbFPC4 on TbBILBO1-NTD, which may provide a basis for rational drug design targeting BILBO1 to combat T. brucei infections.
dc.description.sponsorshipAlliance française contre les maladies parasitaires - ANR-11-LABX-0024en_US
dc.language.isoENen_US
dc.title.enCrystal structure of the N-terminal domain of the trypanosome flagellar protein BILBO1 reveals a ubiquitin fold with a long structured loop for protein binding
dc.typeArticle de revueen_US
dc.identifier.doi10.1074/jbc.RA119.010768en_US
dc.subject.halSciences du Vivant [q-bio]/Biochimie, Biologie Moléculaire/Biologie structurale [q-bio.BM]en_US
dc.subject.halSciences du Vivant [q-bio]/Microbiologie et Parasitologie/Parasitologieen_US
dc.subject.halSciences du Vivant [q-bio]/Microbiologie et Parasitologie/Protistologieen_US
bordeaux.journalJournal of Biological Chemistryen_US
bordeaux.page1489-1499en_US
bordeaux.volume295en_US
bordeaux.hal.laboratoriesMFP (Laboratoire Microbiologie Fondamentale et Pathogénicité) - UMR 5234en_US
bordeaux.issue6en_US
bordeaux.institutionCNRSen_US
bordeaux.peerReviewedouien_US
bordeaux.inpressnonen_US
bordeaux.import.sourcehal
hal.identifierhal-02482599
hal.version1
hal.exportfalse
workflow.import.sourcehal
dc.rights.ccPas de Licence CCen_US
bordeaux.COinSctx_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.jtitle=Journal%20of%20Biological%20Chemistry&rft.date=2020&rft.volume=295&rft.issue=6&rft.spage=1489-1499&rft.epage=1489-1499&rft.eissn=0021-9258&rft.issn=0021-9258&rft.au=VIDILASERIS,%20Keni&LANDREIN,%20Nicolas&PIVOVAROVA,%20Yulia&LESIGANG,%20Johannes&AEKSIRI,%20Niran&rft.genre=article


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