CyaA has two functional domains: the C-terminal domain of about 1300 amino acids, which has membrane-targeting and pore-forming activity, and the 400 amino acid N-terminal domain which has adenylate cyclase enzymatic activity. Intoxication can be triggered by CyaA monomers at low toxin concentrations, whereas cytolytic activity is a co-operative event, mediated by an oligomeric structure consisting of two or more toxin monomers responsible for the production of the pores or channels at higher toxin concentrations
CyaA has two functional domains: the C-terminal domain of about 1300 amino acids, which has membrane-targeting and pore-forming activity, and the 400 amino acid N-terminal domain which has adenylate cyclase enzymatic activity. Intoxication can be triggered by CyaA monomers at low toxin concentrations, whereas cytolytic activity is a co-operative event, mediated by an oligomeric structure consisting of two or more toxin monomers responsible for the production of the pores or channels at higher toxin concentrations
tmAC possessses two homologous large cytoplasmic C-terminal domains, C1 and C2, of about 25 kDA each, which are turned to each other in a head-to-tail manner and forming the acive site and the forskolin binding site, the Gs GTP-binding protein and the Gi GTP-binding protein binding sites, the enzyme also possesses a glycosylated transmembrane domain M2
topology and structure of adenylyl cyclases, mammalian transmembrane adenylyl cyclases share a similar topology of a variable N-terminus and two repeats of a membrane-spanning domain followed by a cytoplasmic domain, the cytoplasmic domains form the catalytic moiety at their interface, creating a pseudosymmetrical site that is primed for bidirectional regulation, crystal structure analysis, overview
tmAC possesses two homologous large cytoplasmic C-terminal domains, C1 and C2, of about 25 kDA each, which are turned to each other in a head-to-tail manner and forming the acive site and the forskolin binding site, the Gs GTP-binding protein and the Gi GTP-binding protein binding sites, the enzyme also possesses a glycosylated transmembrane domain M2
topology and structure of adenylyl cyclases, mammalian transmembrane adenylyl cyclases share a similar topology of a variable N-terminus and two repeats of a membrane-spanning domain followed by a cytoplasmic domain, the cytoplasmic domains form the catalytic moiety at their interface, creating a pseudosymmetrical site that is primed for bidirectional regulation, crystal structure analysis, overview
topology and structure of adenylyl cyclases, mammalian transmembrane adenylyl cyclases share a similar topology of a variable N-terminus and two repeats of a membrane-spanning domain followed by a cytoplasmic domain, the cytoplasmic domains form the catalytic moiety at their interface, creating a pseudosymmetrical site that is primed for bidirectional regulation, crystal structure analysis, overview
topology and structure of adenylyl cyclases, mammalian transmembrane adenylyl cyclases share a similar topology of a variable N-terminus and two repeats of a membrane-spanning domain followed by a cytoplasmic domain, the cytoplasmic domains form the catalytic moiety at their interface, creating a pseudosymmetrical site that is primed for bidirectional regulation, crystal structure analysis, overview
topology and structure of adenylyl cyclases, mammalian transmembrane adenylyl cyclases share a similar topology of a variable N-terminus and two repeats of a membrane-spanning domain followed by a cytoplasmic domain, the cytoplasmic domains form the catalytic moiety at their interface, creating a pseudosymmetrical site that is primed for bidirectional regulation, crystal structure analysis, overview
topology and structure of adenylyl cyclases, mammalian transmembrane adenylyl cyclases share a similar topology of a variable N-terminus and two repeats of a membrane-spanning domain followed by a cytoplasmic domain, the cytoplasmic domains form the catalytic moiety at their interface, creating a pseudosymmetrical site that is primed for bidirectional regulation, crystal structure analysis, overview
topology and structure of adenylyl cyclases, mammalian transmembrane adenylyl cyclases share a similar topology of a variable N-terminus and two repeats of a membrane-spanning domain followed by a cytoplasmic domain, the cytoplasmic domains form the catalytic moiety at their interface, creating a pseudosymmetrical site that is primed for bidirectional regulation, crystal structure analysis, overview
topology and structure of adenylyl cyclases, mammalian transmembrane adenylyl cyclases share a similar topology of a variable N-terminus and two repeats of a membrane-spanning domain followed by a cytoplasmic domain, the cytoplasmic domains form the catalytic moiety at their interface, creating a pseudosymmetrical site that is primed for bidirectional regulation, crystal structure analysis, overview
topology and structure of adenylyl cyclases, mammalian transmembrane adenylyl cyclases share a similar topology of a variable N-terminus and two repeats of a membrane-spanning domain followed by a cytoplasmic domain, the cytoplasmic domains form the catalytic moiety at their interface, creating a pseudosymmetrical site that is primed for bidirectional regulation, crystal structure analysis, overview
tmAC possessses two homologous large cytoplasmic C-terminal domains, C1 and C2, of about 25 kDA each, which are turned to each other in a head-to-tail manner and forming the acive site and the forskolin binding site, the Gs GTP-binding protein and the Gi GTP-binding protein binding sites, the enzyme also possesses a glycosylated transmembrane domain M2
tmAC possessses two homologous large cytoplasmic C-terminal domains, C1 and C2, of about 25 kDA each, which are turned to each other in a head-to-tail manner and forming the acive site and the forskolin binding site, the Gs GTP-binding protein and the Gi GTP-binding protein binding sites, the enzyme also possesses a glycosylated transmembrane domain M2