Journal:JBIC:4
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<applet load="2l0u" size="600" color="" frame="true" spin="on" Scene ="Journal:JBIC:4/Heme_bound_ferro_open/3" align="right" caption="Solved Crystal Structure of Ferrochelatase Mutant"/> | <applet load="2l0u" size="600" color="" frame="true" spin="on" Scene ="Journal:JBIC:4/Heme_bound_ferro_open/3" align="right" caption="Solved Crystal Structure of Ferrochelatase Mutant"/> | ||
=== Bacterial ferrochelatase turns human: Tyr13 determines the apparent metal specificity of Bacillus subtilis ferrochelatase === | === Bacterial ferrochelatase turns human: Tyr13 determines the apparent metal specificity of Bacillus subtilis ferrochelatase === | ||
| - | <big>Mattias D. Hansson • Tobias Karlberg • Christopher A. G. So ̈derberg • Sreekanth Rajan • | + | <big>Mattias D. Hansson • Tobias Karlberg • Christopher A. G. So ̈derberg • Sreekanth Rajan • Martin J. Warren • Salam Al-Karadaghi • Stephen E. J. Rigby • Mats Hansson</big> |
<hr/> | <hr/> | ||
<b>Molecular Tour</b><br> | <b>Molecular Tour</b><br> | ||
| - | Ferrochelatase produces <scene name='Journal:JBIC:4/Heme_bound_ferro/5'>heme by insertion of iron into protoporphyrin IX</scene>. It can also <scene name='Journal:JBIC:4/Copper_protorphyrin/4'>insert other metal ions</scene>. However, the ability to insert other metal ions is species specific. In this way '''Bacillus subtilis''' ferrochelatase can | + | Ferrochelatase produces <scene name='Journal:JBIC:4/Heme_bound_ferro/5'>heme by insertion of iron into protoporphyrin IX</scene>. It can also <scene name='Journal:JBIC:4/Copper_protorphyrin/4'>insert other metal ions</scene>. However, the ability to insert other <scene name='Journal:JBIC:4/Bound_cu_por/5'>metal ions is species specific</scene>. In this way '''Bacillus subtilis''' ferrochelatase can scene name='Journal:JBIC:4/Bound_cu_por/4'>insert copper into protoporphyrin IX</scene>, but to a much less extent cobalt. In contrast, the human and '''Saccharomyces cerevisiae ferrochelatases''' <scene name='Journal:JBIC:4/Co_chelo_bound/4'>prefer cobalt over copper</scene>. <scene name='Journal:JBIC:4/Iron_binding/9'>Our structural work shows that one His residue and one Glu residue are direct ligands to the metal ion</scene>. A third residue, Tyr in B. subtilis ferrochelatase and <scene name='Journal:JBIC:4/Iron_bound_met/2'>Met in human/S. cerevisiae ferrochelatase,</scene> is a third ligand via a water molecule. In the structures of the ferrochelatases the Tyr/Met occupies the same position. We also know that the Tyr residue of the <scene name='Journal:JBIC:4/Bound_cu_por/5'>B. subtilis enzyme</scene> is a <scene name='Journal:JBIC:4/Bound_cu_por/4'>direct ligand to a copper-porphyrin reaction product</scene>. By site directed mutagenesis we changed the Tyr to a Met residue and showed that the metal specificity changed so that the modified B. subtilis ferrochelatase preferred cobalt over copper. Two crystal structures are presented. <scene name='Journal:JBIC:4/Iron_binding_zoomout/3'>One shows</scene> how <scene name='Journal:JBIC:4/Iron_binding_zoomout/1'>a metal ion (iron) is coordinated in the active site of the '''B. subtilis''' ferrochelatase</scene>. The <scene name='Journal:JBIC:4/Bound_cu_por/5'>other shows</scene> how a <scene name='Journal:JBIC:4/Bound_cu_por/4'>copper in a reaction product (copper-mesoporphyrin) is coordinated by the Tyr residue</scene> in the B. subtilis enzyme. |
Revision as of 09:58, 2 November 2010
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Bacterial ferrochelatase turns human: Tyr13 determines the apparent metal specificity of Bacillus subtilis ferrochelatase
Mattias D. Hansson • Tobias Karlberg • Christopher A. G. So ̈derberg • Sreekanth Rajan • Martin J. Warren • Salam Al-Karadaghi • Stephen E. J. Rigby • Mats Hansson
Molecular Tour
Ferrochelatase produces . It can also . However, the ability to insert other . In this way Bacillus subtilis ferrochelatase can scene name='Journal:JBIC:4/Bound_cu_por/4'>insert copper into protoporphyrin IX</scene>, but to a much less extent cobalt. In contrast, the human and Saccharomyces cerevisiae ferrochelatases . . A third residue, Tyr in B. subtilis ferrochelatase and is a third ligand via a water molecule. In the structures of the ferrochelatases the Tyr/Met occupies the same position. We also know that the Tyr residue of the is a . By site directed mutagenesis we changed the Tyr to a Met residue and showed that the metal specificity changed so that the modified B. subtilis ferrochelatase preferred cobalt over copper. Two crystal structures are presented. how . The how a in the B. subtilis enzyme.
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