7EPW

Crystal structure of monooxygenase Tet(X4) with tigecycline

Summary for 7EPW

• Entry DOI: 10.2210/pdb7epw/pdb
• Descriptor: Flavin-dependent monooxygenase, DIHYDROFLAVINE-ADENINE DINUCLEOTIDE, TIGECYCLINE, ... (4 entities in total)
• Functional Keywords: monooxygenase, tet(x4), tigecycline resistance, oxidoreductase
• Biological source: Escherichia coli
• Total number of polymer chains: 1
• Total formula weight: 44719.20

Authors

Cheng, Q.,Chen, S. (deposition date: 2021-04-28, release date: 2021-11-10, Last modification date: 2023-11-29)

Primary citation

Cheng, Q.,Cheung, Y.,Liu, C.,Xiao, Q.,Sun, B.,Zhou, J.,Chan, E.W.C.,Zhang, R.,Chen, S.
Structural and mechanistic basis of the high catalytic activity of monooxygenase Tet(X4) on tigecycline.
Bmc Biol., 19:262-262, 2021

PubMed Abstract: Tigecycline is a tetracycline derivative that constitutes one of the last-resort antibiotics used clinically to treat infections caused by both multiple drug-resistant (MDR) Gram-negative and Gram-positive bacteria. Resistance to this drug is often caused by chromosome-encoding mechanisms including over-expression of efflux pumps and ribosome protection. However, a number of variants of the flavin adenine dinucleotide (FAD)-dependent monooxygenase TetX, such as Tet(X4), emerged in recent years as conferring resistance to tigecycline in strains of Enterobacteriaceae, Acinetobacter sp., Pseudomonas sp., and Empedobacter sp. To date, mechanistic details underlying the improvement of catalytic activities of new TetX enzymes are not available.

PubMed: 34895224
DOI: 10.1186/s12915-021-01199-7

Experimental method

X-RAY DIFFRACTION (2.23 Å)