Fig. 4: Conserved architecture of different tetracycline-inactivating enzymes. | Communications Biology

Fig. 4: Conserved architecture of different tetracycline-inactivating enzymes.

From: Tetracycline-inactivating enzymes from environmental, human commensal, and pathogenic bacteria cause broad-spectrum tetracycline resistance

Fig. 4

Crystal structures of Tet(X7) (a), Tet(X) (b), and Tet(50) (c). All three enzymes have a conserved FAD-binding Rossmann-fold (green), a substrate-binding domain (pink) and a bridge helix (purple). Tet(50) has an additional helix (cyan). The bound FAD is represented spherically. d The Tet(X7) structure is aligned to tigecycline (TIG)-bound Tet(X) structure (PDB ID: 4A6N). Nonbonded interactions of the bound FAD (stick) are conserved between Tet(X7) (blue) and Tet(X). e The nonbonded interactions of tigecycline (TIG) are also conserved between the two proteins.

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