6T4R

Crystal structure of Trypanosoma brucei Morn1

これはPDB形式変換不可エントリーです。

6T4R の概要

• エントリーDOI: 10.2210/pdb6t4r/pdb
• 分子名称: MORN repeat-containing protein 1 (2 entities in total)
• 機能のキーワード: morn repeat, morn1, structural protein, trypanosoma
• 由来する生物種: Trypanosoma brucei
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 49261.51

構造登録者

Grishkovskaya, I.,Kostan, J.,Sajko, S.,Morriswood, B.,Djinovic-Carugo, K. (登録日: 2019-10-14, 公開日: 2020-11-18, 最終更新日: 2024-01-24)

主引用文献

Sajko, S.,Grishkovskaya, I.,Kostan, J.,Graewert, M.,Setiawan, K.,Trubestein, L.,Niedermuller, K.,Gehin, C.,Sponga, A.,Puchinger, M.,Gavin, A.C.,Leonard, T.A.,Svergun, D.I.,Smith, T.K.,Morriswood, B.,Djinovic-Carugo, K.
Structures of three MORN repeat proteins and a re-evaluation of the proposed lipid-binding properties of MORN repeats.
Plos One, 15:e0242677-e0242677, 2020

PubMed Abstract: MORN (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.

PubMed: 33296386
DOI: 10.1371/journal.pone.0242677

実験手法

X-RAY DIFFRACTION (2.352 Å)