Potassium Acts as a GTPase-Activating Element on Each Nucleotide-Binding Domain of the Essential Bacillus subtilis EngA
Figure 8
Superimposition of GD1 or GD2 domains and sequence conservation in the switch 2 motifs.
A, the EngA GD1 domain is depicted in orange and the GDP molecule in cyan. Gln61 from hRas is shown in turquoise, MnmE Glu282 and GDP-AlFx transition state analogue are shown in green. T. maritima EngA Asp55 and Asp61 are shown in purple. Structure superpositions were performed by superimposition of the G1, G4 and G5 motifs using PyMol. B, the EngA GD2 domain is depicted in yellow with its bound GDP molecule shown in cyan. T. maritima EngA Asp55 is shown in purple. Putative Mg2+ position, as obtained from the superposed MnmE structure, is shown in pale green. Hydrogen bonds are depicted with cyan dashed lines. Structure superpositions were performed by superimposition of the G1, G4 and G5 motifs. One hundred EngA sequences were used to show the sequence variation in the switch 2 following the G3 motif and using the WebLogo server (http://weblogo.berkeley.edu/).