1K3S
Type III Secretion Chaperone SigE
Summary for 1K3S
Entry DOI | 10.2210/pdb1k3s/pdb |
Descriptor | SigE, PHOSPHATE ION (3 entities in total) |
Functional Keywords | type iii, secretion, chaperone, sige |
Biological source | Salmonella enterica |
Cellular location | Cytoplasm : O30917 |
Total number of polymer chains | 2 |
Total formula weight | 25895.02 |
Authors | Bertero, M.G.,Luo, Y.,Frey, E.A.,Pfuetzner, R.A.,Wenk, M.R.,Creagh, L.,Marcus, S.L.,Lim, D.,Finlay, B.B.,Strynadka, N.C.J. (deposition date: 2001-10-03, release date: 2001-11-28, Last modification date: 2016-05-25) |
Primary citation | Luo, Y.,Bertero, M.G.,Frey, E.A.,Pfuetzner, R.A.,Wenk, M.R.,Creagh, L.,Marcus, S.L.,Lim, D.,Sicheri, F.,Kay, C.,Haynes, C.,Finlay, B.B.,Strynadka, N.C. Structural and biochemical characterization of the type III secretion chaperones CesT and SigE. Nat.Struct.Biol., 8:1031-1036, 2001 Cited by PubMed Abstract: Several Gram-negative bacterial pathogens have evolved a type III secretion system to deliver virulence effector proteins directly into eukaryotic cells, a process essential for disease. This specialized secretion process requires customized chaperones specific for particular effector proteins. The crystal structures of the enterohemorrhagic Escherichia coli O157:H7 Tir-specific chaperone CesT and the Salmonella enterica SigD-specific chaperone SigE reveal a common overall fold and formation of homodimers. Site-directed mutagenesis suggests that variable, delocalized hydrophobic surfaces observed on the chaperone homodimers are responsible for specific binding to a particular effector protein. Isothermal titration calorimetry studies of Tir-CesT and enzymatic activity profiles of SigD-SigE indicate that the effector proteins are not globally unfolded in the presence of their cognate chaperones. PubMed: 11685226DOI: 10.1038/nsb717 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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