Journal:Acta Cryst F:S2053230X22006586
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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 ''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. | + | 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. <span class="bg-yellow"><span class="far fa-hand-point-right"></span> Remember to drag the structures with the mouse to rotate them.</span> |
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> | ||
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