Journal:JBIC:4
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
| - | <applet load="2l0u" size="600" color="" frame="true" spin="on" Scene ="Journal:JBIC:4/Heme_bound_ferro_open/ | + | <applet load="2l0u" size="600" color="" frame="true" spin="on" Scene ="Journal:JBIC:4/Heme_bound_ferro_open/2" 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 • 5 Martin J. Warren • Salam Al-Karadaghi • Stephen E. J. Rigby • Mats Hansson</big> | <big>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</big> | ||
| Line 5: | Line 5: | ||
<b>Molecular Tour</b><br> | <b>Molecular Tour</b><br> | ||
| - | Ferrochelatase produces <scene name='Journal:JBIC:4/Heme_bound_ferro/ | + | 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 insert copper,<scene name='Journal:JBIC:4/Co_chelo_bound/3'>but to a much less extent cobalt</scene>. In contrast, the human and Saccharomyces cerevisiae ferrochelatases prefer cobalt over copper. <scene name='Journal:JBIC:4/Iron_binding/7'>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 <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 other shows how a <scene name='Journal:JBIC:4/Bound_cu_por/2'>copper in a reaction product (copper-mesoporphyrin) is coordinated by the Tyr residue</scene> in the B. subtilis enzyme. |
Revision as of 10:58, 31 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
Ferrochelatase produces . It can also . However, the ability to insert other metal ions is species specific. In this way Bacillus subtilis ferrochelatase can insert copper,. 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 . The other shows how a in the B. subtilis enzyme.
Proteopedia Page Contributors and Editors (what is this?)
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.
