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![[Figure 2]](mn5078fig2_combined_mag.jpg)
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Figure 2
Interactions between CoA and NAT enzymes. (a) Upper panel, alignment of the active sites of wild-type apo (RHILO)NAT1 (pink; PDB entry 2bsz) and the apo and holo (RHILO)NAT1 F42W mutant (brown and blue, respectively). Lower panel, interactions between the `P-loop' residues of the holo (RHILO)NAT1 F42W mutant and bound CoA. Hydrogen bonds are shown as dashed lines. (b) Details of the interaction between CoA (cyan) and the holo (RHILO)NAT1 F42W mutant (grey). Hydrogen bonds are shown as dashed lines. (c) Amino-acid sequence alignment of (RHILO)NAT1 (blue), (MYCMR)NAT1 (purple), (HUMAN)NAT2 (green) and (BACAN)NAT1 (grey). Residues interacting with CoA are shown in background colours. The catalytic triad Cys–His–Asp is indicated by stars. Boxed residues correspond to the `mammalian/eukaryotic insertion loop' between β8 and β9 [with the secondary structure of (RHILO)NAT1 as a reference]. (d) CoA conformations from cofactor-bound structures of (RHILO)NAT1 (blue), (MYCMR)NAT1 (purple; PDB entry 2vfc), (HUMAN)NAT2 (green; PDB entry 2pfr) and (BACAN)NAT1 (grey; PDB entry 3lnb). The four structures were aligned and only the catalytic cysteine residue is shown (labelled Cys). (e) Superposition of holo (RHILO)NAT1 F42W (blue) and (MYCMR)NAT1 (purple) showing the alignment of CoA molecules (r.m.s.d. 1.14 Å). The catalytic triad residues Cys, His and Asp are shown. |
![[Figure 2]](mn5078fig2_combined.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
