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. The crystal structure of the CtcP protein from ''Streptomyces aureofaciens'' ([[7xgb]]) is shown in cartoon representation in two different views:
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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 protein from ''Streptomyces aureofaciens'' ([[7xgb]]) is shown in <scene name='91/915821/Cv/4'>cartoon representation</scene>, The N- (green) and C- (blue) terminal domains of CtcP are color coded.
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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. 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.
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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. <jmol><jmolButton><script>display:A</script><text>only CtcP</text></jmolButton><jmolButton><script>display:B</script><text>only PltM</text></jmolButton><jmolButton><script>display all</script><text>both CtcP and PltM</text></jmolButton></jmol>
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. <jmol><jmolButton><script>display:A</script><text>only CtcP</text></jmolButton><jmolButton><script>display:B</script><text>only PltM</text></jmolButton><jmolButton><script>display all</script><text>both CtcP and PltM</text></jmolButton></jmol>

Revision as of 07:22, 30 June 2022

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Proteopedia Page Contributors and Editors (what is this?)

Alexander Berchansky, Jaime Prilusky

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.
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