3GYZ

Crystal structure of IpgC from Shigella flexneri

3GYZ の概要

• エントリーDOI: 10.2210/pdb3gyz/pdb
• 関連するPDBエントリー: 3GZ1 3GZ2
• 分子名称: Chaperone protein ipgC, SULFATE ION, GLYCEROL, ... (5 entities in total)
• 機能のキーワード: asymmetric homodimer, tetratricopeptide repeat, tpr, 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: 2
• 化学式量合計: 35282.63

構造登録者

Lunelli, M.,Lokareddy, R.K.,Zychlinsky, A.,Kolbe, M. (登録日: 2009-04-06, 公開日: 2009-06-16, 最終更新日: 2024-05-29)

主引用文献

Lunelli, M.,Lokareddy, R.K.,Zychlinsky, A.,Kolbe, M.
IpaB-IpgC interaction defines binding motif for type III secretion translocator
Proc.Natl.Acad.Sci.USA, 106:9661-9666, 2009

PubMed Abstract: The delivery of virulence factors into host cells through type III secretion systems is essential for enterobacterial pathogenesis. Molecular chaperones bind specifically to virulence factors in the bacterial cytosol before secretion. Invasion plasmid gene C (IpgC) is a chaperone that binds 2 essential virulence factors of Shigella: invasion plasmid antigens (Ipa) B and C. Here, we report the crystal structure of IpgC alone and in complex with the chaperone binding domain (CBD) of IpaB. The chaperone captures the CBD in an extended conformation that is stabilized by conserved residues lining the cleft. Analysis of the cocrystal structure reveals a sequence motif that is functional in the IpaB translocator class from different bacteria as determined by isothermal titration calorimetry. Our results show how translocators are chaperoned and may allow the design of inhibitors of enterobacterial diseases.

PubMed: 19478065
DOI: 10.1073/pnas.0812900106

実験手法

X-RAY DIFFRACTION (2.15 Å)