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Figure 7 | BMC Structural Biology

Figure 7

From: Structural basis for hypermodification of the wobble uridine in tRNA by bifunctional enzyme MnmC

Figure 7

Multiple sequence alignments of bifunctional MnmC. Amino acid seuences of seven bacterial MnmC ( Escherichia coli, Yersinia pestis, Salmonella enterica, Klebsiella pneumoniae, Pectobacterium carotovorum, Vibrio cholerae, and Haemophilus influenza) are aligned and compared. Residue numbering and secondary structural elements are based on ecMnmC. Residues contributing to the interdomain interface in Table 2 are marked in purple circles, where purple H denotes those residues which are involved in hydrogen bonds at the interface. Green diamonds highlighted the residues shown in Figure 3, which form the binding pocket for SAM in ecMnmC. Residues shown in Figure 4 which form hydrogen bonds with FAD are labeled with orange squares.

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