On the Structure and Function of the Phytoene Desaturase CRTI from Pantoea ananatis, a Membrane-Peripheral and FAD-Dependent Oxidase/Isomerase
Figure 10
Structural alignment of CRTI with five FAD-binding Rossmann fold proteins (Pfam:CL0063) identified by a DALI search.
The proteins are Methanosarcina mazei oxidoreductase (RMSD 4.6; 3 KA7; Seetharaman et al., unpublished), Myxococcus xanthus protoporphyrinogen oxidase (RMSD 4.6; 2 IVD; Corradi et al., 2006), Nicotiana tabacum mitochondrial protoporphyrinogen IX oxidase (RMSD 4.8; ISEZ; Koch et al., 2004), Bacillus subtilis protoporphyrinogen oxidase (RMSD 5.3, 3I6D, Qin et al., 2010) and Rhodococcus opacus L-amino acid oxidase (RMSD 4.8; 2JB2; Faust et al., 2007). The secondary structure elements of CRTI have been indicated above the alignment and the colored bar underneath the alignment indicates the domain organisation with the FAD-binding domain (green), the substrate-binding domain (blue), and the non-conserved ‘helical’ or ‘membrane-binding’ domain (orange). Disordered regions in the structure are represented by a dotted line and putative FAD binding residues are indicated by purple circles (hydrophobic interactions) and triangles (hydrophilic interactions). This figure was generated with TEXshade [60].