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Fig. S1. SPR control experiments performed with two distinct His-tagged bacterial proteins whose function is not related to peptidoglycan biosynthesis. MurE, MurF and control proteins 1 and 2 were injected at a concentration of 600 nM over immobilized MurG and MreB as described in Experimental procedures. Controls 1 and 2 did not display any binding to neither MurG nor MreB whereas MurE and MurF clearly interacted with both immobilized proteins.

Fig. S2. Superposition of the structures of MurE from T. maritima (orange, in complex with ADP) and E. coli (1E8C; cyan), with the product of the reaction, present only in the structure of MurE from E. coli, shown as sticks. Note that the conformation of the C-terminal domain in both molecules is comparable, despite the fact that only the E. coli enzyme was crystallized in the presence of the reaction product.

Fig. S3. Superposition of the structures of MurD from T. maritima (blue) and from E. coli (yellow), the latter having been crystallized in the presence of UMA (1UAG). Note that the N-terminal and central domains superpose well, while the C-terminal domain displays considerable conformational flexibility.

Table S1. MurF data collection, phasing, molecular replacement and structure refinement statistics.

Table S2. MurE data collection, phasing, molecular replacement and structure refinement statistics.

Table S3. MurD data collection, phasing, molecular replacement and structure refinement statistics.

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