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Figure 1
Crystal structure of abMurG. (a) Overview of the function of MurG. (b) Size-exclusion chromatography profile. Two peaks are labeled corresponding to an oligomer and a dimer. SDS–PAGE to assess the identity and purity is shown to the right of the two main peaks. The loaded fractions are indicated by black and red bars. (c) Native PAGE gel. The loaded samples are indicated above the gel. (d) Multi-colored cartoon representation of monomeric abMurG. The chain from the N- to C-terminus is colored from blue to red. Helices and sheets are labeled α and β, respectively. (e) A cartoon representation of the structure of abMurG showing the domain boundary in the structure. (f) Cartoon representation of the three abMurG molecules in an asymmetric unit. (g) Superposition of the structures of the molecules found in one asymmetric unit. (h) Putty representation showing the B-factor distribution. Rainbow colors from red to violet with increasing B-factor values were used for B-factor visualization.

Volume 8| Part 4| July 2021| Pages 574-583
ISSN: 2052-2525