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Literature summary extracted from

  • Allison, S.E.; Tuinema, B.R.; Everson, E.S.; Sugiman-Marangos, S.; Zhang, K.; Junop, M.S.; Coombes, B.K.
    Identification of the docking site between a type III secretion system ATPase and a chaperone for effector cargo (2014), J. Biol. Chem., 289, 23734-23744.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
7.4.2.8 recombinant expression of FLAG-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) Salmonella enterica

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
7.4.2.8 purified recombinant wild-type enzyme, hanging drop vapor diffusion method, mixing of 0.002 ml of 1.7 mg/ml protein in 20 mM Tris, pH 7.5, 0.1 M potassium chloride, and 0.01 M tris(2-carboxyethyl)phosphine with 0.001 ml of crystallization solution containing 0.5 M ammonium sulfate, 0.1 M sodium citrate tribasic dihydrate, pH 5.6, and 10% v/v Jeffamine M-600, and 200 nl of 0.1 M L-proline, the drops are initially dehydrated against 0.5 ml of 1.5 M ammonium sulfate, X-ray diffraction structure determination and analysis at 2.1 A resolution, molecular replacement and modeling Salmonella enterica

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
7.4.2.8 Mg2+ required Salmonella enterica

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
7.4.2.8 ATP + H2O Salmonella enterica
-
ADP + phosphate
-
?
7.4.2.8 additional information Salmonella enterica T3SS ATPases functions as a docking site for chaperone-effector complexes, molecular mechanism by which SsaN captures these complexes to initiate translocation and recognizes the chaperones, overview. Modeling of the interaction between the multicargo chaperone, SrcA, and enzyme SsaN and validation of the model using SrcA mutagenesis to identify the residues on both the chaperone and ATPase that mediate the interaction ?
-
?

Organism

EC Number Organism UniProt Comment Textmining
7.4.2.8 Salmonella enterica P74857 serovar Typhimurium, gene SPI-2
-

Purification (Commentary)

EC Number Purification (Comment) Organism
7.4.2.8 recombinant FLAG-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by affinity chromatography Salmonella enterica

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
7.4.2.8 ATP + H2O
-
Salmonella enterica ADP + phosphate
-
?
7.4.2.8 additional information T3SS ATPases functions as a docking site for chaperone-effector complexes, molecular mechanism by which SsaN captures these complexes to initiate translocation and recognizes the chaperones, overview. Modeling of the interaction between the multicargo chaperone, SrcA, and enzyme SsaN and validation of the model using SrcA mutagenesis to identify the residues on both the chaperone and ATPase that mediate the interaction Salmonella enterica ?
-
?

Synonyms

EC Number Synonyms Comment Organism
7.4.2.8 SsaN
-
Salmonella enterica
7.4.2.8 T3SS ATPase
-
Salmonella enterica
7.4.2.8 type III secretion system ATPase
-
Salmonella enterica

General Information

EC Number General Information Comment Organism
7.4.2.8 additional information enzyme structure molecular modeling, overview Salmonella enterica
7.4.2.8 physiological function Gram-negative pathogens utilize type III secretion systems (T3SSs) to inject bacterial effector proteins into the host. An important component of T3SSs is a conserved ATPase that captures chaperone-effector complexes and energizes their dissociation to facilitate effector translocation. Chaperones engage type III secretion system ATPases to facilitate effector secretion, molecular basis of the chaperone-T3SS ATPase interaction interface, modeling of the interaction between the multicargo chaperone, SrcA, and the enzyme SsaN, overview. Importance of the chaperone-T3SS ATPase interaction for the pathogenesis of Salmonella Salmonella enterica