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Literature summary for 7.4.2.8 extracted from

  • Chen, L.; Ai, X.; Portaliou, A.G.; Minetti, C.A.; Remeta, D.P.; Economou, A.; Kalodimos, C.G.
    Substrate-activated conformational switch on chaperones encodes a targeting signal in type III secretion (2013), Cell Rep., 3, 709-715.
    View publication on PubMedView publication on EuropePMC

Localization

Localization Comment Organism GeneOntology No. Textmining
cytoplasm a peripheral membrane protein located at the cytoplasmic side Escherichia coli 5737
-
membrane a peripheral membrane protein located at the cytoplasmic side Escherichia coli 16020
-

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
350000
-
about Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + H2O Escherichia coli
-
ADP + phosphate
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli
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enteropathogenic
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O
-
Escherichia coli ADP + phosphate
-
?

Subunits

Subunits Comment Organism
hexamer full-length EscN forms a stable hexamer in solution with stimulated ATPase activity Escherichia coli

Synonyms

Synonyms Comment Organism
EscN
-
Escherichia coli
EscN ATPase
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Escherichia coli
TTS ATPase
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Escherichia coli

General Information

General Information Comment Organism
malfunction abrogation of the interaction between the CesAB–EspA complex and EscN resulted in severe secretion and infection defects Escherichia coli
additional information a recombinant well folded CesAB D14L/R18D/E20L mutant homodimer variant binds specifically to EscN in contrast to the monomeric form Escherichia coli
physiological function the enzyme is the key protein in the type III secretion (TTS) system, a multi-protein machinery that has evolved to deliver bacterial virulence proteins directly into eukaryotic cells, through an organelle termed the injectisome. The ATPase EscN is a peripheral membrane protein located at the entrance of the injectisome, at the cytoplasmic base of the injectisome, and forms a ring structure. Enzyme EscN selectively engages the EspA-loaded CesAB, but not the unliganded CesAB. The targeting signal is encoded in a disorder-order structural transition in CesAB that is elicited only upon binding of its physiological substrate, EspA. There is no interaction between CesAB and EscN, CesAB appears not to be engaged by the injectisome ATPase in its substrate-free form, but the CesAB–EspA heterodimer interacts specifically with the EscN ATPase mediated by CesAB. Efficient targeting of CesAB-EspA to ATPase EscN is required for EspA secretion Escherichia coli