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. 2014 Dec 29;112(2):E119–E126. doi: 10.1073/pnas.1415908112

Fig. 6.

Fig. 6.

The structure of Mtb CrgA as a platform for assembling other interacting proteins. (A) Schematic view of the likely binding sites for five cell division proteins known to interact with CrgA. FtsZ and FtsI interact with the cytoplasmic N terminus of CrgA. CwsA and FtsQ have binding motifs in their transmembrane (TM) helices and are therefore likely to interact with the CrgA TM helices. PBPA has no such binding motif in its TM helix and a minimalistic N-terminal sequence and therefore is hypothesized to interact with the CrgA interhelical loop. (B) A structural model of the CrgA–FtsQ complex. TM1 and TM2 of CrgA are shown as cyan and pink ribbons, respectively. FtsQ is shown as spheres. Residues involved in binding are shown as red spheres (Thr78 and Gly85) and blue ball-and-stick (Phe81 and Met82) on the CrgA side and as green spheres (Gly16, Gly12, and Ala9) on the FtsQ side.