journal menu
![[Figure 4]](mn5119fig4mag.jpg)
|
|
Figure 4
Structural comparison between FadB and the FadB2 dimer. (a) Ribbon diagram of Mtb FadB (PDB entry 4b3h; Venkatesan & Wierenga, 2013) coloured according to its structural domains. HAD, 3-hydroxyacyl dehydrogenase domain. (b) The same as in (a), but superimposed on Mtb FadB2 (magenta) by secondary-structure matching. Light blue and yellow spheres indicate the location of the active site in the HAD domain. (c, d) Adding the second protomer of the FadB2 dimer demonstrates the superposition of the FadB2 C-terminal domain (grey) with the HAD-C2 domain of FadB. The FadB hydratase domain is omitted from the view. (e) Close-up view of the central area of the FadB2 dimer and its match with the HAD-C1 and HAD-C2 domains of FadB. (f) Superposition of the HAD-C1 and HAD-C2 domains of FadB. Residues numbers of the N- and C-terminal residues of the structural fragments are indicated in addition to secondary-structure labels. |
![[Figure 4]](mn5119fig4.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
Open 
access
access
