Journal:JBIC:4
From Proteopedia
| Line 5: | Line 5: | ||
<b>Molecular Tour</b><br> | <b>Molecular Tour</b><br> | ||
| - | <scene name='Journal:JBIC:4/Opening/1'>Ferrochelatase</scene> produces <scene name='Journal:JBIC:4/Heme_bound_ferro/4'>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 insert copper, but to a much less extent cobalt. In contrast, the human and Saccharomyces cerevisiae ferrochelatases prefer cobalt over copper. <scene name='Journal:JBIC:4/Iron_binding/3'>Our structural work shows that one His residue and one Glu residue are direct ligands to the metal ion</scene>. A third residue, <scene name='Journal:JBIC:4/Iron_bound_met/2'>Tyr in B. subtilis ferrochelatase and 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 B. subtilis enzyme is a direct ligand to a copper-porphyrin reaction product. 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 Proteopedia structures are presented. One shows how a metal ion (iron) is coordinated in the active site of the B. subtilis ferrochelatase. The other shows how a copper in a reaction product (copper-mesoporphyrin) is coordinated by the Tyr residue in the B. subtilis enzyme. | + | <scene name='Journal:JBIC:4/Opening/1'>Ferrochelatase</scene> produces <scene name='Journal:JBIC:4/Heme_bound_ferro/4'>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 insert copper, but to a much less extent cobalt. In contrast, the human and Saccharomyces cerevisiae ferrochelatases prefer cobalt over copper. <scene name='Journal:JBIC:4/Iron_binding/3'>Our structural work shows that one His residue and one Glu residue are direct ligands to the metal ion</scene>. A third residue, <scene name='Journal:JBIC:4/Iron_bound_met/2'>Tyr in B. subtilis ferrochelatase and 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 B. subtilis enzyme is a direct ligand to a copper-porphyrin reaction product. 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 Proteopedia structures are presented. One shows how a metal ion (iron) is coordinated in the active site of the B. subtilis ferrochelatase. The other shows how a <scene name='Journal:JBIC:4/Bound_cu_por/1'>copper in a reaction product (copper-mesoporphyrin) is coordinated by the Tyr residue</scene> in the B. subtilis enzyme. |
To Proteopedia: I think a good complement to our article would be two Proteopedia structures with 1) B. subtilis ferrochelatase with bound iron in the active site (bound to residues H183, E264 and indirect to Y13) and 2) B. subtilis ferrochelatase with bound copper-porphyrin in the active site (bound to Y13). These structure have PDB accession numbers 2HK6 and 1C9E, respectively. The file uploaded below is to make it clear to you what the copper-porphyrin bound to Y13 looks like. | To Proteopedia: I think a good complement to our article would be two Proteopedia structures with 1) B. subtilis ferrochelatase with bound iron in the active site (bound to residues H183, E264 and indirect to Y13) and 2) B. subtilis ferrochelatase with bound copper-porphyrin in the active site (bound to Y13). These structure have PDB accession numbers 2HK6 and 1C9E, respectively. The file uploaded below is to make it clear to you what the copper-porphyrin bound to Y13 looks like. | ||
Revision as of 11:08, 28 October 2010
|
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 • 5 Martin J. Warren • Salam Al-Karadaghi • Stephen E. J. Rigby • Mats Hansson
Molecular Tour
produces . It can also . However, the ability to insert other metal ions is species specific. In this way Bacillus subtilis ferrochelatase can insert copper, but to a much less extent cobalt. In contrast, the human and Saccharomyces cerevisiae ferrochelatases prefer cobalt over copper. . A third residue, 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 B. subtilis enzyme is a direct ligand to a copper-porphyrin reaction product. 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 Proteopedia structures are presented. One shows how a metal ion (iron) is coordinated in the active site of the B. subtilis ferrochelatase. The other shows how a in the B. subtilis enzyme.
To Proteopedia: I think a good complement to our article would be two Proteopedia structures with 1) B. subtilis ferrochelatase with bound iron in the active site (bound to residues H183, E264 and indirect to Y13) and 2) B. subtilis ferrochelatase with bound copper-porphyrin in the active site (bound to Y13). These structure have PDB accession numbers 2HK6 and 1C9E, respectively. The file uploaded below is to make it clear to you what the copper-porphyrin bound to Y13 looks like.
