3GZ1
Crystal structure of IpgC in complex with the chaperone binding region of IpaB
Summary for 3GZ1
| Entry DOI | 10.2210/pdb3gz1/pdb |
| Related | 3GYZ 3GZ2 |
| Descriptor | Chaperone protein ipgC, Invasin ipaB, GLYCEROL, ... (4 entities in total) |
| Functional Keywords | tetratricopeptide repeat, tpr, chaperone, chaperone binding region, virulence, membrane, secreted, transmembrane |
| Biological source | Shigella flexneri More |
| Total number of polymer chains | 4 |
| Total formula weight | 39404.46 |
| Authors | Lunelli, M.,Lokareddy, R.K.,Zychlinsky, A.,Kolbe, M. (deposition date: 2009-04-06, release date: 2009-06-16, Last modification date: 2023-11-01) |
| 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 Cited by 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: 19478065DOI: 10.1073/pnas.0812900106 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.15 Å) |
Structure validation
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