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. 2023 Jul 5;13:1204707. doi: 10.3389/fcimb.2023.1204707

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Copyright © 2023 Bachmaier, Gould, Polatoglou, Omelianczyk, Brennand, Aloraini, Munday, Horn, Boshart and de Koning

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Sequence comparisons (A, C) of the predicted phosphate binding cassettes (PBCs) of T. brucei CARP1 (A, CNBD-A, -B, -C) or CARP11 (C) with Escherichia coli CRP (EcCRP), Mus musculus EPAC2 (MmEpac2) and Bos taurus PKARIα (BtPKARIα). The amino acid numbers of the predicted sequence insertions within the CARP11 PBC are indicated below the alignment. Asterisks indicate conserved Glu and Arg residues known to be essential for cAMP binding (Berman et al., 2005). (B, D) Structural alignments of CARP1 CNBD-A (B, dark blue) or CARP11 CNBD (D, dark blue) with BtPKARIa CNBD-A (PDB 1RGS, black) and EcCRP CNBD (PDB 4N9H, green) with the conserved arginines R320 of CARP1 and R520 of CARP11, respectively, overlaying the conserved arginines R211 of BtPKARIa CNBD-A and R82 of EcCRP CNBD. The structures were retrieved from http://wheelerlab.net/alphafold/ and superimposed with Pymol version 2.5.4.