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A more recent structure of a high affinity ( K d 100 nM) 1:1 complex between MeaB and the Cbl-binding domain of an MCM, solved in the presence of GMPPCP, reveals a completely different dimer conformation, where the two nucleotides are now quite close to one another, sandwiched at the dimer interface, with the switch III loop now engaged in direct interactions with the nucleotide of the opposite protomer of MeaB, effectively burying the bound GTP (Figure 43B)

Complete resolution of symptoms after one treatment was reported in 10 of 12 patients

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The bursa allows muscles and tendons to easily glide over boney prominences