Journal:Acta Cryst F:S2053230X22006586
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| - | + | <StructureSection load='' size='450' side='right' scene='91/915821/Cv/1' caption=''> | |
===Crystal structure determination of the halogenase CtcP from ''Streptomyces aureofaciens''=== | ===Crystal structure determination of the halogenase CtcP from ''Streptomyces aureofaciens''=== | ||
<big>Lijuan Yin</big> <ref>doi: 10.1107/S2053230X22006586</ref> | <big>Lijuan Yin</big> <ref>doi: 10.1107/S2053230X22006586</ref> | ||
<hr/> | <hr/> | ||
<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'' ([[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> |
| - | ''Streptomyces aureofaciens'' ([[7xgb]]) is shown in | + | |
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| - | <scene name='91/915821/Cv/ | + | 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> |
| - | '' | + | <scene name='91/915821/Cv/11'>The comparison of the substrates binding site in both CtcP and PltM</scene>. 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. <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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<b>References</b><br> | <b>References</b><br> | ||
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