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Figure 3 | BMC Microbiology

Figure 3

From: Structural analysis of FAD synthetase from Corynebacterium ammoniagenes

Figure 3

Alignments. (A) Structural alignment of the N-terminal domain of the CaFADS model (residues 19–186) with the corresponding regions of TmFADS and several NTs. Residues proposed to be involved in particular substrate binding are marked as; for phosphate groups, ✳ ribose or ▲ adenine portions of ATP. denotes regions where substrates specific for each enzyme have been reported to interact. (B) Structural alignment of the C-terminal domain (residues 187–338) of the C. ammoniagenes FADS model with those of TmFADS and RFKs from S. pombe and H. sapiens. Residues proposed to be involved in particular substrate binding are marked as; for phosphate groups, ✳ ribose or ▲ adenine portions of ATP and, for the phosphate, ribityl or ■ isoalloxazine ring portions of RF. Each template is referred to its pdb code according to Table 1. Residues involved in substrate binding in each particular structure are shown in bold case. Consensus sequences are shown below alignment, Φ, Ψ and Ω denoting hydrophobic, polar and any residue, respectively. Secondary structure prediction of CaFADS, obtained using the JOY server [36] and visual inspection, is shown above each alignment, with β signifying β-strand residues and α signifying α-helix residues.

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