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![[Figure 6]](jv5004fig6_combined_mag.jpg)
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Figure 6
Structure-based sequence alignment and comparison of structural elements of CtFDO with the most similar structures of GMC oxidoreductases. (a) Structure-based sequence alignment of CtFDO (PDB entry 6ze2, chain A) with MtAAO (PDB entry 6o9n), AfGDH (PDB entry 4ynt), AnGOX (PDB entry 1cf3), PaGOX (PDB entry 1gpe, chain A) and PeAAO (PDB entry 3fim) according to PDBeFold (Krissinel & Henrick, 2005  ). Black and blue backgrounds show invariant residues of these six enzymes and the conserved motifs (Gly-X-Gly-X-X-Gly sequence motif and the conserved histidine residue) indicative of GMC oxidoreductases, respectively. The second residue of the His–His/His–Ser pair is shown in white letters on a magenta background. A pink background denotes other residues present in the active site. The parts of the sequence shown on a light brown background correspond to the main secondary-structure differences between the compared enzymes and CtFDO. The extra secondary-structure elements of CtFDO are coloured red and blue. The yellow, red and orange colours mark the secondary-structure elements of the wide-open access to the active site in CtFDO. The confirmed N-glycosylation sites in CtFDO and structurally confirmed N-glycosylation sites in MtAAO, AfGDH and AnGOX are marked by cyan boxes. The vicinal disulfide in CtFDO is marked by red stars. The graphics were created in ESPript (Robert & Gouet, 2014). (b) Secondary-structure representation of CtFDO:free with highlighted structural motifs as marked in the structure-based sequence alignment. The active-site pocket is shown in surface representation (green; calculated by HOLLOW; Ho & Gruswitz, 2008). The FAD cofactor is represented in sticks with C atoms coloured magenta. Molecular graphics were created with PyMOL (Schrödinger). |
![[Figure 6]](jv5004fig6_combined.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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