3GYZ

Crystal structure of IpgC from Shigella flexneri

Summary for 3GYZ

• Entry DOI: 10.2210/pdb3gyz/pdb
• Related: 3GZ1 3GZ2
• Descriptor: Chaperone protein ipgC, SULFATE ION, GLYCEROL, ... (5 entities in total)
• Functional Keywords: asymmetric homodimer, tetratricopeptide repeat, tpr, chaperone, virulence
• Biological source: Shigella flexneri
• Cellular location: Cytoplasm: P0A2U4
• Total number of polymer chains: 2
• Total formula weight: 35282.63

Authors

Lunelli, M.,Lokareddy, R.K.,Zychlinsky, A.,Kolbe, M. (deposition date: 2009-04-06, release date: 2009-06-16, Last modification date: 2024-05-29)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.15 Å)