Fig. 8: RlpA and its recruitment of binding-partners for the divisome during daughter-cell separation. | Communications Biology

Fig. 8: RlpA and its recruitment of binding-partners for the divisome during daughter-cell separation.

From: In vitro studies of the protein-interaction network of cell-wall lytic transglycosylase RlpA of Pseudomonas aeruginosa

Fig. 8

This perspective illustrates a single snapshot of the entire daughter-cell-separation process. The placement of RlpA and select binding partners spatially demonstrate the interrelationship of such protein–protein interactions for the purposes of peptidoglycan denuding, orthogonal growth of the peptidoglycan, and as components for the multi-enzyme divisome complex. C2 symmetry within the septum is shown. “LT” placeholder can equate to LT binding partners; SltB1, SltB2, SltB3, MltA, MltB, MltD, MltF, or MltF2.

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