Pseudomonas aeruginosa Exopolyphosphatase Is Also a Polyphosphate: ADP Phosphotransferase

Figure 4

Sequence alignment of the connecting peptide between subdomains II and III. (a) Alignment of the end of N-ecPp and N-paPp. Sequences were aligned using ClustalX. The arrow indicates the cleavage site for both N-terminal variants used in this work N-paPp and N-paPp. (b) Logo for paPpx peptide 301–326. Residues 303–315 constitute the last α-helix of N-terminal domain. Residues 316–320 constitute the loop connecting the N-terminal domain to the C-terminal domain. Residues 321–326 are forming the first α-helix of C-terminal domain. 599 sequences aligned with Clustal were used to create the logo. (c) Cartoon representation of the closed conformation of N-paPpx in superimposition to N-ecPpx (PDB: 1U6Z). Residues of active site are represented as sticks and Mg²⁺ ion is represented as a green sphere. Color references: N-ecPpx: green: subdomain I, blue: subdomain II, and red: α-helix formed by residues 297–310. N-paPpx: yellow: subdomain I, cyan: subdomain II, and coral: α-helix formed by residues 303–315.

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