6SJQ

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

6SJQ の概要

• エントリーDOI: 10.2210/pdb6sjq/pdb
• 関連するPDBエントリー: 2MEK
• 分子名称: Flagellar pocket-related cytoskeletal protein, GLYCEROL (3 entities in total)
• 機能のキーワード: bilbo1, ubiquitin fold, flagellar pocket collar, parasite, peptide binding protein
• 由来する生物種: Trypanosoma brucei
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14200.86

構造登録者

Vidilaseris, K.,Dong, G. (登録日: 2019-08-13, 公開日: 2020-01-01, 最終更新日: 2024-05-15)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.604 Å)