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. 2022 Jul 26;13:942482. doi: 10.3389/fimmu.2022.942482

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Copyright © 2022 Ries, Heß, Nouri, Wichelhaus, Göttig, Falcone and Kraiczy

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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Structural prediction of CipA obtained with AlphaFold2. The mature CipA_18-369 protein has a short, 11 amino acid-long unstructured N-terminus (A), followed by three approximately equally sized domains (B), recognized as META domain 1 (AA 46-107), META domain 2 (AA 151-253) and a C-terminal domain of unknown function, DUF4377 (AA 277-361). The DUF4377 domain is made up entirely of beta-sheets, the last of which contains the E360 residue in WT CipA (blue, E360 highlighted in yellow in (C) which was mutagenized to proline in the E360P mutant (beige, P360 highlighted in red in (C). Introduction of this amino acid disrupts the final beta-sheet strands and results in reorientation of the last 9 C-terminal amino acids (D), away from the DUF4377 domain, but without any overt effect on the other parts of the molecule.