Figure 2.
Fig. 2. Overall structure of E. coli FabH . A, ribbon
diagram of the FabH monomer. The N-terminal (1-170) and
C-terminal (171-317) halves have a similar fold. The core
secondary structural elements are labeled as b1-b5 and a1-a3,
respectively and referred in the text with a prefix of N or C to
indicate the domain they belong to. These -sheet and
-helices
are drawn in magenta (N, b1-b5), cyan (N, a1-a3), red (C,
b1-b5), and blue (C, a1-a3). N is the N terminus, which precedes
N, b1. C is the C terminus, which comes off C, b5. Secondary
elements of insertion regions are drawn in yellow and orange for
N- and C-terminal domains, respectively. The catalytic Cys112 is
shown in a red ball-and-stick drawing, and the CoA molecule
(green) was taken from the acetyl-CoA complex structure to
orient the view. B, stereo view of the superposition between the
N-terminal (red) and C-terminal (blue) domains of FabH. Core
-strands are
labeled; the overlay was generated by matching the 33 -carbon
pairs from four of the strands.
-sheet and
-helices
are drawn in magenta (N, b1-b5), cyan (N, a1-a3), red (C,
b1-b5), and blue (C, a1-a3). N is the N terminus, which precedes
N, b1. C is the C terminus, which comes off C, b5. Secondary
elements of insertion regions are drawn in yellow and orange for
N- and C-terminal domains, respectively. The catalytic Cys112 is
shown in a red ball-and-stick drawing, and the CoA molecule
(green) was taken from the acetyl-CoA complex structure to
orient the view. B, stereo view of the superposition between the
N-terminal (red) and C-terminal (blue) domains of FabH. Core