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 |
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 |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
7.4.2.8 | Mg2+ | required | Salmonella enterica |
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 | ? | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
7.4.2.8 | Salmonella enterica | P74857 | serovar Typhimurium, gene SPI-2 | - |
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 |
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 | ? | - |
? |
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 |
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 |