2RJI

Malarial EBA-175 region VI crystallographic structure reveals a KIX-like binding interface

2RJI の概要

• エントリーDOI: 10.2210/pdb2rji/pdb
• 関連するPDBエントリー: 1sb0
• 分子名称: Erythrocyte binding antigen 175, CALCIUM ION (3 entities in total)
• 機能のキーワード: cbp kix, eba-175, plasmodium falciparum, region vi, protein transport, cell invasion
• 由来する生物種: Plasmodium falciparum (malaria parasite P. falciparum)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 20060.56

構造登録者

Withers-Martinez, C.,Blackman, M.J. (登録日: 2007-10-15, 公開日: 2007-11-27, 最終更新日: 2024-10-16)

主引用文献

Withers-Martinez, C.,Haire, L.F.,Hackett, F.,Walker, P.A.,Howell, S.A.,Smerdon, S.J.,Dodson, G.G.,Blackman, M.J.
Malarial EBA-175 Region VI Crystallographic Structure Reveals a KIX-Like Binding Interface
J.Mol.Biol., 375:773-781, 2008

PubMed Abstract: The malaria parasite proliferates in the bloodstream of its vertebrate host by invading and replicating within erythrocytes. To achieve successful invasion, a number of discrete and essential events need to take place at the parasite-host cell interface. Erythrocyte-binding antigen 175 (EBA-175) is a member of a family of Plasmodium falciparum erythrocyte-binding proteins involved in the formation of a tight junction, a necessary step in invasion. Here we present the crystal structure of EBA-175 region VI (rVI), a cysteine-rich domain that is highly conserved within the protein family and is essential for EBA-175 trafficking. The structure was solved by selenomethionine single-wavelength anomalous dispersion at 1.8 A resolution. It reveals a homodimer, containing in each subunit a compact five-alpha-helix core that is stabilized by four conserved disulfide bridges. rVI adopts a novel fold that is likely conserved across the protein family, indicating a conserved function. It shows no similarity to the Duffy-binding-like domains of EBA-175 involved in erythrocyte binding, indicating a distinct role. Remarkably, rVI possesses structural features related to the KIX-binding domain of the coactivator CREB-binding protein, supporting the binding and trafficking roles that have been ascribed to it and providing a rational basis for further experimental investigation of its function.

PubMed: 18036613
DOI: 10.1016/j.jmb.2007.10.071

実験手法

X-RAY DIFFRACTION (1.8 Å)