Journal:Acta Cryst F:S2053230X22006586

spinqualitylabelsall models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Crystal structure determination of the halogenase CtcP from Streptomyces aureofaciens Lijuan Yin 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 cartoon representation, 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 FAD-binding pocket and an active center. 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 comparison of the substrates binding site in both CtcP and 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

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