1K3E

Type III secretion chaperone CesT

Summary for 1K3E

• Entry DOI: 10.2210/pdb1k3e/pdb
• Descriptor: CesT (1 entity in total)
• Functional Keywords: chaperone, secretion, type iii, intimin receptor
• Biological source: Escherichia coli O157:H7
• Cellular location: Cytoplasm : Q47015
• Total number of polymer chains: 2
• Total formula weight: 35389.75

Authors

Luo, Y.,Bertero, M.,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: 2001-10-02, release date: 2001-11-28, Last modification date: 2024-02-07)

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

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: 11685226
DOI: 10.1038/nsb717

Experimental method

X-RAY DIFFRACTION (2.8 Å)