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. Author manuscript; available in PMC: 2025 Oct 1.
Published in final edited form as: Mol Oral Microbiol. 2024 Mar 4;39(5):354–367. doi: 10.1111/omi.12458

Figure 3. Sequence and structural comparison of TDE1909 to CdaA proteins.

Figure 3.

(A) The protein sequence for TDE1909 was aligned to the CdaA sequence from L. monocyotgenes (LmCdaA) and S. pneumoniae using Clustal X. Highly conserved regions involved in metal coordination in the binding site are highlighted in red boxes. (B) The predicted structure of TDE1909 (cyan) from AlphaFold2 was aligned to the structure of LmCdaA (gray) co-crystallized with ATP (PDB: 8C4O) using PyMol. The Co+2 ions are magenta, the ATP bound to LmCdaA is blue and the conserved regions on both TDE1909 and LmCdaA are red.