Extended Data Fig. 10: The MBOAT proteins in non-Dlt pathway cell envelope acylation systems have additional C-terminal helices that allow the C-terminal motif of these proteins to nestle into the active site. | Nature Microbiology

Extended Data Fig. 10: The MBOAT proteins in non-Dlt pathway cell envelope acylation systems have additional C-terminal helices that allow the C-terminal motif of these proteins to nestle into the active site.

From: Mechanism of d-alanine transfer to teichoic acids shows how bacteria acylate cell envelope polymers

Extended Data Fig. 10

Alignments of predicted structures of MBOAT proteins from bacterial cell envelope polymer acetylation systems (and a system of unknown function in archaea) with the predicted structure of the DltBX complex show that the non-DltB MBOAT proteins likely share a similar architecture to DltB but with a C-terminal extension of several additional helices. All of the predicted structures here were generated using the ColabFold implementation of AlphaFold2 and aligned using the PyMOL ‘super’ command.

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