3KS2

Crystal Structure of Type-III Secretion Chaperone IpgC from Shigella flexneri (residues 10-155)

3KS2 の概要

• エントリーDOI: 10.2210/pdb3ks2/pdb
• 関連するPDBエントリー: 3gyz
• 分子名称: Chaperone protein ipgC (1 entity in total)
• 機能のキーワード: tpr motif, chaperone, virulence
• 由来する生物種: Shigella flexneri
• 細胞内の位置: Cytoplasm: P0A2U4
• タンパク質・核酸の鎖数: 18
• 化学式量合計: 308328.23

構造登録者

Geisbrecht, B.V.,Barta, M.L. (登録日: 2009-11-20, 公開日: 2010-08-25, 最終更新日: 2023-11-01)

主引用文献

Barta, M.L.,Zhang, L.,Picking, W.L.,Geisbrecht, B.V.
Evidence for alternative quaternary structure in a bacterial Type III secretion system chaperone
Bmc Struct.Biol., 10:21-21, 2010

PubMed Abstract: Type III secretion systems are a common virulence mechanism in many Gram-negative bacterial pathogens. These systems use a nanomachine resembling a molecular needle and syringe to provide an energized conduit for the translocation of effector proteins from the bacterial cytoplasm to the host cell cytoplasm for the benefit of the pathogen. Prior to translocation specialized chaperones maintain proper effector protein conformation. The class II chaperone, Invasion plasmid gene (Ipg) C, stabilizes two pore forming translocator proteins. IpgC exists as a functional dimer to facilitate the mutually exclusive binding of both translocators.

PubMed: 20633281
DOI: 10.1186/1472-6807-10-21

実験手法

X-RAY DIFFRACTION (3.3 Å)