3KS2

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

Summary for 3KS2

Entry DOI	10.2210/pdb3ks2/pdb
Related	3gyz
Descriptor	Chaperone protein ipgC (1 entity in total)
Functional Keywords	tpr motif, chaperone, virulence
Biological source	Shigella flexneri
Cellular location	Cytoplasm: P0A2U4
Total number of polymer chains	18
Total formula weight	308328.23
Authors	Geisbrecht, B.V.,Barta, M.L. (deposition date: 2009-11-20, release date: 2010-08-25, Last modification date: 2023-11-01)
Primary citation	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 Cited by 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 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (3.3 Å)

Structure validation