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Fig. 4. | BMC Biology

Fig. 4.

From: Structural and mechanistic basis of the high catalytic activity of monooxygenase Tet(X4) on tigecycline

Fig. 4.

Structural comparison of Tet(X4)-tigecycline complex with Tet(X4) and Tet(X2)-tigecycline complex. A Cartoon and superimposition of Tet(X4)-tigecycline structure (the color of the cartoon is shown in yellow) and Tet(X4) structure (the color of the cartoon is shown in blue). The red dashed box indicates the dynamic changes in the loop between α10 and α11, with details shown in the right enlarged dashed box. FAD and T1C are shown as sticks. B Superposition of the structure of Tet(X4)-tigecycline complex (the color of the cartoon is shown in yellow) with the Tet(X2)-tigecycline complex (4A6N, the color of the cartoon is shown in cyan). The black dashed box indicates the interactions of TIC with Tet(X4) and Tet(X2), with details shown in the right enlarged dashed box. T1C are shown as sticks; conserved interacting residues are depicted as lines

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BMC Biology

ISSN: 1741-7007

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