Genetic and Biochemical Characterization of the MinC-FtsZ Interaction in Bacillus subtilis (original) (raw)
Figure 6
The binding site for MinC differs in B. subtilis and E. coli FtsZ.
A. Comparison between mutations that promote MinC resistance in B. subtilis (red residues) and E. coli (blue residues) mapped onto the 2VAM FtsZ structure [75]. E. coli residue N280 corresponds to B. subtilis D280; E276 corresponds to Q276; R271 corresponds to S271. Two other important landmarks are highlighted in the structure: catalytic residue D213, shown in yellow, defines the center of the FtsZ-FtsZ interface (the polymerization axis follows a vertical line through this residue); and the point where the CTP should emerge from the structure (residue F315) is shown in orange. B. Surface electrostatic potential of B. subtilis FtsZ (2VAM) obtained with the “protein contact potential” tool of PyMOL. Note that the MinC binding site corresponds to a highly negative region of the FtsZ molecule.