6SJQ

1.7-A resolution crystal structure of the N-terminal domain of T. brucei BILBO1

Summary for 6SJQ

• Entry DOI: 10.2210/pdb6sjq/pdb
• Related: 2MEK
• Descriptor: Flagellar pocket-related cytoskeletal protein, GLYCEROL (3 entities in total)
• Functional Keywords: bilbo1, ubiquitin fold, flagellar pocket collar, parasite, peptide binding protein
• Biological source: Trypanosoma brucei
• Total number of polymer chains: 1
• Total formula weight: 14200.86

Authors

Vidilaseris, K.,Dong, G. (deposition date: 2019-08-13, release date: 2020-01-01, Last modification date: 2024-05-15)

Primary citation

Vidilaseris, K.,Landrein, N.,Pivovarova, Y.,Lesigang, J.,Aeksiri, N.,Robinson, D.R.,Bonhivers, M.,Dong, G.
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.
J.Biol.Chem., 295:1489-1499, 2020

PubMed Abstract: is a protist parasite causing sleeping sickness and nagana in sub-Saharan Africa. 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 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 infections.

PubMed: 31882537
DOI: 10.1074/jbc.RA119.010768

Experimental method

X-RAY DIFFRACTION (1.604 Å)