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![[Figure 3]](mn5119fig3mag.jpg)
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Figure 3
Multiple sequence alignment of FadB homologues. Secondary-structure elements of M. tuberculosis FadB2 and FadB (determined by DSSP; Kabsch & Sander, 1983  ) are indicated above and below the sequences, respectively, with α, β and η indicating α-helices, β-strands and 310-helices, respectively. The boundary between the N- and C-terminal domains is indicated as N | C. Conserved residues are highlighted in red text surrounded by blue boxes; residues that are identical across the alignment are shown in white on a red background. The @ and ^ symbols indicate residues in human L-3-hydroxyacyl-CoA dehydrogenase (HsHAD; PDB entry 1f0y; Barycki et al., 2000) within a 4.0 Å radius of the CoA and NAD+ ligands, respectively. FadB2, M tuberculosis FadB2 (Rv0468); FadB3, M tuberculosis FadB3 (Rv1715); FadB_Pfr, Pseudomonas fragi fatty-acid oxidation complex FadB (α-subunit; WP_010656816); FadB, Mtb trifunctional fatty-acid oxidation protein complex (Rv0860; PDB entry 4b3h; Venkatesan & Wierenga, 2013). Inset: alignment of C-terminal residues 629–720 of FadB with residues 190–268 of FadB2 as derived from the structural superposition shown in Fig. 4(e). |
![[Figure 3]](mn5119fig3.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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