Journal:Acta Cryst F:S2053230X22006586

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<b>Molecular Tour</b><br>
<b>Molecular Tour</b><br>
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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. Although FAD is not observed in the structure, the monooxygenase domain has a conserved FAD-binding pocket and an active center.
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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:
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*<scene name='91/915821/Cv/4'>1st view</scene>.
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*<scene name='91/915821/Cv/3'>2nd view</scene>.
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Although FAD is not observed in the structure, the monooxygenase domain has a conserved FAD-binding pocket and an active center.
<b>References</b><br>
<b>References</b><br>

Revision as of 15:15, 26 June 2022

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