 | Acta Crystallographica Section F Acta Crystallographica Section F STRUCTURAL BIOLOGY COMMUNICATIONS |
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![[Figure 1]](no5208fig1mag.jpg)
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Figure 1
The crystal structure of the truncated form of L. monocytogenes CdaA, lacking the first 100 N-terminal residues and abbreviated Δ100. (a) The biochemical reaction catalyzed by diadenylate cyclase (DAC) involves the formation of cyclic di-AMP (c-di-AMP). (b) A cartoon representation depicting the catalytically active Δ100 CdaA dimer in its postcatalytic state with c-di-AMP bound in the active site (PDB entry 6hvl). (c) Superposition of BsCdaA (gray) and LmCdaA (pale green; PDB entry 8c4p) reveals an identical binding mode of the lead compound previously designed for LmCdaA (Compound 7). The polder omit map (marine) is contoured at the +3σ level. The numbering corresponds to BsCdaA. |
![[Figure 1]](no5208fig1.jpg)
| STRUCTURAL BIOLOGY COMMUNICATIONS |
ISSN: 2053-230X
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