Extended Data Fig. 3: Electrostatic surface rendering of ACP1-KS-AT domains.
From: Structure and dynamics of the essential endogenous mycobacterial polyketide synthase Pks13
(a) The KS-AT surface is colored by electrostatic potential (red: acidic, blue: basic) of the residues. ACP1a and ACP1b and their ensuing linkers to the KS (yellow and lemon chiffon) are superimposed onto the KS-AT electrostatic potential surface, illustrating that the DE-rich linker lie near positively charged surfaces on the KS. (b) ACP1a, ACP1b, and the linkers to the KS are colored by electrostatic potential (red: acidic, blue: basic) of the residues. Model of KS-AT is superimposed onto the highly negative electrostatic potential surface of the DE-rich linker.
