Fig. 3: Superimposition of a selection of ACPs on holo-ACP5b.
From: Decrypting the programming of β-methylation in virginiamycin M biosynthesis
a Superimposition of the average NMR structures of virginiamycin holo-ACP5a (in deep blue), holo-ACP6 (in white) and holo-ACP7 (in firebrick red) on the crystal structure of holo-ACP5b (in lime green). α-helices are shown in cartoon representation and the Ppant cofactor as sticks. b Superimposition of the NMR structures of the tandem ACPs of MmpA module 3, Mup ACP3a (in marine blue) and ACP3b (in orange) (PDB ID: 2L22), on the crystal structure of holo-ACP5b (in lime green) (PDB ID: 8AHQ), reveals r.m.s.d. of 0.949 Å (67 Cα) and 1.106 Å (59 Cα), respectively, and no substantial deviation in terms of the helix α3 orientation. The tryptophan flags of Mup ACP3a and ACP3b10 and the corresponding phenylalanine of Vir ACP5b, are shown in ball-and-stick representation.
