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- Bacillus1
- c-di-AMP1
- CdaA catalytic domain1
- CdaACD1
- crystallography1
- cyclic dinucleotide1
- cyclic-di-adenosine monophosphate1
- DAC1
- DacA catalytic domain1
- DacACD1
- diadenylate cyclase1
- microscale thermophoresis1
- MST1
- normalized spatial discrepancy1
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- protein structure1
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- signaling1
- small-angle X-ray scattering data1
Microbiology
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- Research ArticleOpen Access
Structural basis for the inhibition of the Bacillus subtilis c-di-AMP cyclase CdaA by the phosphoglucomutase GlmM
Journal of Biological ChemistryVol. 297Issue 5101317Published online: October 19, 2021- Monisha Pathania
- Tommaso Tosi
- Charlotte Millership
- Fumiya Hoshiga
- Rhodri M.L. Morgan
- Paul S. Freemont
- and others
Cited in Scopus: 2Cyclic-di-adenosine monophosphate (c-di-AMP) is an important nucleotide signaling molecule that plays a key role in osmotic regulation in bacteria. c-di-AMP is produced from two molecules of ATP by proteins containing a diadenylate cyclase (DAC) domain. In Bacillus subtilis, the main c-di-AMP cyclase, CdaA, is a membrane-linked cyclase with an N-terminal transmembrane domain followed by the cytoplasmic DAC domain. As both high and low levels of c-di-AMP have a negative impact on bacterial growth, the cellular levels of this signaling nucleotide are tightly regulated.