MurG

=__MurG__=

MurG is an essential glycosyltransferase, which catalyses the final step of peptidoglycan synthesis and the formation of the lipid II precursor (Mohammadi et al, 2007).

It has been domonstrated that MurG is required for cell growth and survival. In addition, it is conserved between eubacteria further highlighting the importance of its function (Mohammadi et al, 2007). As there is no MurG counterpart in mammalian cells, this enzyme is of particular interest as a potential antibiotic target.
 * __Functions:__**


 * __Structure:__**

Immunoblotting studies have shown MurG to be tightly associated with the cytoplasmic membrane of E. coli cells. It appears to be randomly distributed within the cell envelope, but is present at a relatively higher intensity at the division site. However, this localisation to the division site is dependant on the presence of the divisome complex (Mohammadi et al, 2007).
 * __Location:__**

Studies with truncated forms of MurG have indicated the C-terminal 66 amino acids of MurG are essential to its membrane association, either through direct interactions with the membrane components, or because their absence affects the folding of MurG.

MurG is present in 1,200 (+/- 33) molecules per average E. coli K-12 wildtype cell (Mohammadi et al, 2007).

MurG has been shown to interact with the MreB and MraY proteins in vivo (Mohammadi et al, 2007).
 * __Interactions:__**