5KE1

Structure of a C-terminal fragment of the IcsA/VirG passenger-domain

5KE1 の概要

• エントリーDOI: 10.2210/pdb5ke1/pdb
• 分子名称: Outer membrane protein IcsA autotransporter, NICKEL (II) ION (3 entities in total)
• 機能のキーワード: virulence factor, autochaperone, autotransporter, transport protein
• 由来する生物種: Shigella flexneri
• 細胞内の位置: Outer membrane protein IcsA autotransporter: Periplasm. Outer membrane protein IcsA: Secreted. Outer membrane protein IcsA translocator: Cell outer membrane ; Multi-pass membrane protein : Q7BCK4
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 73261.85

構造登録者

Leupold, S.,Scrima, A. (登録日: 2016-06-09, 公開日: 2017-03-15, 最終更新日: 2024-01-10)

主引用文献

Leupold, S.,Busing, P.,Mas, P.J.,Hart, D.J.,Scrima, A.
Structural insights into the architecture of the Shigella flexneri virulence factor IcsA/VirG and motifs involved in polar distribution and secretion.
J. Struct. Biol., 198:19-27, 2017

PubMed Abstract: IcsA/VirG is a key virulence factor of the human pathogen Shigella flexneri, acting as both an adhesin and actin-polymerizing factor during infection. We identified a soluble expression construct of the IcsA/VirG α-domain using the ESPRIT library screening system and determined its structure to 1.9Å resolution. In addition to the previously characterized autochaperone domain, our structure reveals a new domain, which shares a common fold with the autochaperone domains of various autotransporters. We further provide insight into the previously structurally uncharacterized β-helix domain that harbors the polar targeting motif and passenger-associated transport repeat. This structure is the first of any member of the recently identified passenger-associated transport repeat-containing autotransporters. Thus, it provides new insights into the overall architecture of this class of autotransporters, the function of the identified additional autochaperone domain and the structural properties of motifs involved in polar targeting and secretion of the Shigella flexneri virulence factor IcsA/VirG.

PubMed: 28268178
DOI: 10.1016/j.jsb.2017.03.003

実験手法

X-RAY DIFFRACTION (1.9 Å)