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![[Figure 2]](ji5017fig2mag.jpg)
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Figure 2
Structure-based alignment of the amino-acid sequence of Janthinobacterium sp. J3 ferredoxin reductase (CARDO-RJ3; UniProt entry Q84II0) with related sequences. Structural alignment with carbazole 1,9a-dioxygenase ferredoxin reductase from Pseudomonas resinovorans CA10 (CARDO-RCA10; UniProt entry Q84GI4), toluene 4-monooxygenase NADH oxidoreductase from P. mendocina (T4moF; PDB entry 4wqm), benzoate dioxygenase reductase from Acinetobacter baylyi ADP1 (BZDO-R; PDB entry 1krh), phthalate dioxygenase reductase from P. cepacia (PDO-R; PDB entry 2pia), naphthalene dioxygenase reductase from P. putida (NDO-R; UniProt entry Q52126) and the FNR–ferredoxin complex from maize leaf (FdxRed; PDB entry 1gaq) was performed using PROMALS3D (Pei et al., 2008  ). Secondary-structure assignments and the colour scheme are based on the CARDO-RJ3 structure (Fig. 1a). The red and orange columns indicate completely conserved and highly homologous amino-acid residues, respectively. The C-terminal ferredoxin-like domain (beginning at Thr236) of PDO-R aligns with the N-terminal ferredoxin-like domains (Fd domains) of the other reductase sequences. The solid green arrows show the four cysteine ligands of the [2Fe–2S] cluster. Light blue solid arrows indicate residues with direct side-chain hydrogen bonds to FAD, and the solid black arrows indicate aromatic residues that exhibit stacking interactions with FAD. The purple arrows show the amino-acid residues that form hydrogen bonds to NADH via their side chains in the docking simulation. |
![[Figure 2]](ji5017fig2.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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