دورية أكاديمية
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
| العنوان: | 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 |
|---|---|
| المؤلفون: | VIDILASERIS, Keni, LANDREIN, Nicolas, PIVOVAROVA, Yulia, LESIGANG, Johannes, AEKSIRI, Niran, ROBINSON, Derrick, BONHIVERS, Melanie, DONG, Gang |
| سنة النشر: | 2020 |
| مصطلحات موضوعية: | Sciences du Vivant [q-bio]/Biochimie, Biologie Moléculaire/Biologie structurale [q-bio.BM], Sciences du Vivant [q-bio]/Microbiologie et Parasitologie/Parasitologie, Sciences du Vivant [q-bio]/Microbiologie et Parasitologie/Protistologie |
| الوصف: | Trypanosoma 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. ; Alliance française contre les maladies parasitaires |
| نوع الوثيقة: | article in journal/newspaper |
| اللغة: | English |
| تدمد: | 0021-9258 |
| العلاقة: | https://oskar-bordeaux.fr/handle/20.500.12278/182399Test |
| DOI: | 10.1074/jbc.RA119.010768 |
| الإتاحة: | https://doi.org/20.500.12278/182399Test https://doi.org/10.1074/jbc.RA119.010768Test https://oskar-bordeaux.fr/handle/20.500.12278/182399Test https://hdl.handle.net/20.500.12278/182399Test |
| حقوق: | open ; Pas de Licence CC |
| رقم الانضمام: | edsbas.32EB3F53 |
| قاعدة البيانات: | BASE |
Full Text Finder | تدمد: | 00219258 |
|---|---|
| DOI: | 10.1074/jbc.RA119.010768 |