2019-10-31 19:52:262025-05-14 20:00:20
The protein
Effectors of protein activity
the interaction with [[protein|CdaR]] controls the diadenylate cyclase activity of [[protein|CdaA]] [Pubmed|23192352]
the interaction with [[protein|CdaR]] inhibits the diadenylate cyclase activity of [[protein|CdaA]] (shown in S. aureus) [pubmed|30668586]
the interaction with [[protein|CdaR]] controls the diadenylate cyclase activity of [[protein|CdaA]] [Pubmed|23192352]
the interaction with [[protein|CdaR]] inhibits the diadenylate cyclase activity of [[protein|CdaA]] (shown in S. aureus) [pubmed|30668586]
the interaction with [[protein|GlmM]] inhibits the diadenylate cyclase activity of [[protein|CdaA]] under conditions of osmotic stress (shown in L. monocytogenes) [pubmed|32250026]
The protein
Structure
[PDB|4RV7] (the [SW|DAC domain] and C-terminal domain of CdaA from ''Listeria monocytogenes'' (aa 101 - 273), 65% identity) [Pubmed|25605729]
[PDB|6HVL] (the [SW|DAC domain] and C-terminal domain of CdaA from ''Listeria monocytogenes'' (aa 101 - 273) in complex with c-di-AMP, 65% identity) [Pubmed|31118276]
[PDB|6HUW]
[PDB|4RV7] (the [SW|DAC domain] and C-terminal domain of CdaA from ''Listeria monocytogenes'' (aa 101 - 273), 65% identity) [Pubmed|25605729]
[PDB|6HVL] (the [SW|DAC domain] and C-terminal domain of CdaA from ''Listeria monocytogenes'' (aa 101 - 273) in complex with c-di-AMP, 65% identity) [Pubmed|31118276]
References
Reviews
References
Original publications
labs
[SW|Jörg Stülke], University of Göttingen, Germany [http://genmibio.uni-goettingen.de Homepage]