Figure 2.
Fig. 2. Structure of LpxD. (A) Ribbon diagram of a subunit.
The UBD is yellow, the LBD is blue, loops are magenta, and the
HE is red. Selected elements of secondary structure are labeled,
and the coils are numbered. (B) The trimer. The view is parallel
to the noncrystallographic symmetry threefold axis. Subunits are
colored gray, wheat, and slate, and the domains of the gray
subunit are labeled. UDP-GlcNAc (complex II) is represented by
spheres, and palmitic acid is represented by sticks. The atoms
of the ligands are colored as follows: C, green; N, blue; O,
red; P, yellow. (C) Orthogonal view of the trimer. (D) Primary
and secondary structure. -strands are depicted by
arrows, and -helices are depicted
by cylinders. Colors are as described in A. Disordered residues
at the C terminus are marked by dots. Highly conserved residues
(>60% identity in 85 sequences) are highlighted in gray, and
strictly conserved residues (100% identity) are in black. Green
stars and circles indicate residues that interact with
UDP-GlcNAc and palmitic acid, respectively. Salmon boxes
represent sites of conditionally lethal point mutations in E.
coli and S. typhimurium LpxD.
-strands are depicted by
arrows, and 
-helices are depicted
by cylinders. Colors are as described in A. Disordered residues
at the C terminus are marked by dots. Highly conserved residues
(>60% identity in 85 sequences) are highlighted in gray, and
strictly conserved residues (100% identity) are in black. Green
stars and circles indicate residues that interact with
UDP-GlcNAc and palmitic acid, respectively. Salmon boxes
represent sites of conditionally lethal point mutations in E.
coli and S. typhimurium LpxD.