Journal:Acta Cryst F:S2053230X22006586
From Proteopedia
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<b>Molecular Tour</b><br> | <b>Molecular Tour</b><br> | ||
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 | 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'' is shown in cartoon representation in two different views: | + | ''Streptomyces aureofaciens'' ([[7xgb]]) is shown in cartoon representation in two different views: |
*<scene name='91/915821/Cv/4'>1st view</scene>. | *<scene name='91/915821/Cv/4'>1st view</scene>. | ||
*<scene name='91/915821/Cv/3'>2nd view. Rotated ~ 90° clockwise around the horizontal axis, respective to the orientation shown at 1st view</scene>. The N- (green) and C- (blue) terminal domains of CtcP are color coded. | *<scene name='91/915821/Cv/3'>2nd view. Rotated ~ 90° clockwise around the horizontal axis, respective to the orientation shown at 1st view</scene>. The N- (green) and C- (blue) terminal domains of CtcP are color coded. | ||
| - | Although FAD is not observed in the structure, the monooxygenase domain has a conserved FAD-binding pocket and an active center. | + | Although FAD is not observed in the structure, the monooxygenase domain has a conserved <scene name='91/915821/Cv/9'>FAD-binding pocket and an active center</scene>. 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. |
<b>References</b><br> | <b>References</b><br> | ||
Revision as of 11:02, 28 June 2022
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This page complements a publication in scientific journals and is one of the Proteopedia's Interactive 3D Complement pages. For aditional details please see I3DC.
