7XGB

Crystal structure of the ctcP from Streptomyces aureofaciens

Summary for 7XGB

• Entry DOI: 10.2210/pdb7xgb/pdb
• Descriptor: Tetracycline 7-halogenase (2 entities in total)
• Functional Keywords: ctcp, streptomyces aureofaciens, flavoprotein
• Biological source: Kitasatospora aureofaciens
• Total number of polymer chains: 4
• Total formula weight: 254191.69

Authors

Yin, L. (deposition date: 2022-04-04, release date: 2022-07-20, Last modification date: 2024-11-13)

Primary citation

Yin, L.
Crystal structure determination of the halogenase CtcP from Streptomyces aureofaciens.
Acta Crystallogr.,Sect.F, 78:270-275, 2022

PubMed Abstract: Chlortetracycline (CTC), a derivative of tetracycline (TC), is a broadly used antibiotic that inhibits the synthesis of bacterial proteins by competing with the A-site tRNA on ribosomes. A recent study showed that during the biosynthesis of CTC in Streptomyces aureofaciens, the halogenase CtcP catalyzes the final chlorination reaction and transforms TC into CTC. However, the structure of this fundamental enzyme is still lacking. Here, selenomethionine-derivatized CtcP from S. aureofaciens was overexpressed and purified and its structure was determined at 2.7 Å resolution. The structure of CtcP reveals the conserved monooxygenase domain shared by all flavin-dependent halogenases and a unique C-terminal domain. Although FAD was not observed in the structure, the monooxygenase domain has a conserved FAD-binding pocket and active center. The C-terminal domain displays an α-helical bundle fold, which could contribute to substrate specificity. This work provides a molecular basis for enzyme engineering to improve the industrial production of CTC.

PubMed: 35787554
DOI: 10.1107/S2053230X22006586

Experimental method

X-RAY DIFFRACTION (2.7 Å)