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1K3S

Type III Secretion Chaperone SigE

Summary for 1K3S
Entry DOI10.2210/pdb1k3s/pdb
DescriptorSigE, PHOSPHATE ION (3 entities in total)
Functional Keywordstype iii, secretion, chaperone, sige
Biological sourceSalmonella enterica
Cellular locationCytoplasm : O30917
Total number of polymer chains2
Total formula weight25895.02
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 citationLuo, 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: 11685226
DOI: 10.1038/nsb717
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.9 Å)
Structure validation

226707

數據於2024-10-30公開中

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