Crystal structure determination of the halogenase CtcP from Streptomyces aureofaciens
Lijuan Yin [1]
Molecular Tour
The crystal structure of selenomethionine-derivatised Streptomyces aureofaciens halogenase CtcP, which functions in chlortetracycline biosynthesis, is reported here at 2.7 Å resolution. The structure reveals a conserved monooxygenase domain and a unique C-terminal domain. The crystal structure of the CtcP protein from Streptomyces aureofaciens (7xgb) is shown in , The N- (green) and C- (blue) terminal domains of CtcP are color coded. Remember to drag the structures with the mouse to rotate them.
Although FAD is not observed in the structure, the monooxygenase domain has a conserved . All the essential residues which coordinate the FAD in both CtcP and PltM are shown in ball-and-stick representation. CtcP (7xgb) is colored in green, while PltM (6bzq) is colored in white-smoke. The FAD molecule and the Cl- ion are from the model of PltM.
. The enzymatic active center residues (K87 in PltM, K98 in CtcP) and the phloroglucinol from PltM structure are shown in ball-and-stick representation. The CtcP (7xgb) is colored in green and blue, while the PltM (6bza) is colored in white-smoke.
References
- ↑ Yin L. Crystal structure determination of the halogenase CtcP from Streptomyces aureofaciens. Acta Crystallogr F Struct Biol Commun. 2022 Jul 1;78(Pt 7):270-275. doi:, 10.1107/S2053230X22006586. Epub 2022 Jul 4. PMID:35787554 doi:http://dx.doi.org/10.1107/S2053230X22006586
