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![[Figure 2]](mn5119fig2mag.jpg)
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Figure 2
Ribbon representation of the structure of Mtb FadB2. (a) The FadB2 monomer consists of an N-terminal domain (purple–red) with two Rossmann-fold motifs (β1–α1–β2 and β4–α4–β5; cyan), and an α-helical bundle in the C-terminal domain (α7–α11; magenta). The location of the active site is indicated with translucent spheres for CoA and NAD+ (derived from the superposition with ligand-bound HsHAD; PDB entry 1f0y; Barycki et al., 2000  ). Secondary-structure elements are labelled according to the secondary-structure analysis by DSSP (Kabsch & Sander, 1983) as shown in Fig. 3. The locations of the N- and C-termini are indicated with the corresponding residue numbers (1 and 287; bold italics), as is the domain boundary (190). (b) Representation of the three FadB2 dimers in the asymmetric unit of the crystal structure. (c, d) Two orthogonal views of the FadB2 dimer (chains A and B). The dimer interface is formed entirely by the helical C-terminal domain (helices α7–α11). |
![[Figure 2]](mn5119fig2.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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