Ferrochelatase - Revision history

Michal Harel at 08:52, 30 June 2019

Michal Harel — Sun, 30 Jun 2019 08:52:01 GMT

←Older revision		Revision as of 08:52, 30 June 2019
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	</StructureSection>		</StructureSection>

-	==3D structures of ferrochelatase==
-
-	Updated on {{REVISIONDAY2}}-{{MONTHNAME\|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
-	{{#tree:id=OrganizedByTopic\|openlevels=0\|
-
-	*Ferrochelatase
-
-	**[[1ak1]] – BsFECH – ''Bacillus subtilis''<br />
-	**[[2ac4]] - BsFECH (mutant) <br />
-	**[[1doz]] - BsFECH + Mg<br />
-	**[[1ld3]] - BsFECH + Zn<br />
-	**[[2ac2]] - BsFECH (mutant) + Zn<br />
-	**[[2h1v]], [[3goq]] - BsFECH (mutant) + Mg<br />
-	**[[2h1w]] - BsFECH (mutant) + Fe + Mg<br />
-	**[[2hk6]] - BsFECH + Fe+ Mg<br />
-	**[[1n0i]] - BsFECH + Cd + Mg<br />
-	**[[3m4z]] - BsFECH + Co + Mg<br />
-	**[[1l8x]] - yFECH + Co – yeast<br />
-	**[[1lbq]] - yFECH<br />
-	**[[2c8j]] – FECH – ''Bacillus anthracis''<br />
-	**[[2qd4]], [[2hrc]] - hFECH + Fe2S2 - human<br />
-	**[[1hrk]], [[2pnj]], [[2po5]], [[2po7]], [[3aqi]], [[4f4d]], [[3w1w]], [[4mk4]] - hFECH (mutant) + Fe2S2<BR />
-
-	*Ferrochelatase complex with porphyrin
-
-	**[[2qd3]], [[3hcn]], [[3hco]], [[3hcp]] - hFECH + protoporphyrin IX + Fe2S2<BR />
-	**[[4kla]], [[4klc]], [[4klr]], [[4kmm]] - hFECH (mutant) + protoporphyrin IX + Fe2S2<br />
-	**[[3hcr]] - hFECH + protoporphyrin IX + O2 + Fe2S2<BR />
-	**[[2hre]], [[2qd1]], [[2qd2]] - hFECH (mutant) + protoporphyrin IX + Fe2S2<BR />
-	**[[2qd5]] - hFECH + protoporphyrin IX + Pb + Fe2S2<BR />
-	**[[1c1h]] - BsFECH + N-methylmesoporphyrin + Mg<br />
-	**[[2q3j]], [[2q2o]] - BsFECH (mutant) + N-methylmesoporphyrin + Mg<br />
-	**[[2q2n]] – BsFECH + protoporphyrin IX + Mg<br />
-	**[[1c9e]] - BsFECH + N-methylmesoporphyrin + Cu + Mg<br />
-
-	* Sirohydrochlorin ferrochelatase
-
-	**[[5zt8]] – BsSirB <br />
-	**[[5zt7]], [[6jv6]] – BsSirB + Co<br />
-	**[[5zt9]] – BsSirB + Ni<br />
-	**[[5zta]] – BsSirB + Fe<br />
-	}}
	== References ==		== References ==
	<references/>		<references/>
	[[Category:Topic Page]]		[[Category:Topic Page]]

Michal Harel at 08:50, 30 June 2019

Michal Harel — Sun, 30 Jun 2019 08:50:54 GMT

←Older revision		Revision as of 08:50, 30 June 2019
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	<StructureSection load='1c1h' size='350' side='right' scene='52/526342/Cv/1' caption='Ferrochelatase with methylmesoporphyrin and Mg+2 ion (PDB code [[1c1h]])'>		<StructureSection load='1c1h' size='350' side='right' scene='52/526342/Cv/1' caption='Ferrochelatase with methylmesoporphyrin and Mg+2 ion (PDB code [[1c1h]])'>
		+
		+	__TOC__
	== Function ==		== Function ==

Michal Harel at 08:50, 30 June 2019

Michal Harel — Sun, 30 Jun 2019 08:50:30 GMT

←Older revision		Revision as of 08:50, 30 June 2019
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	== Function ==		== Function ==

-	'''Ferrochelatase''' (FECH) catalyzes the last step in the formation of heme. FECH adds Fe+2 to protoporphyrin IX converting it to protoheme. The human FECH is a homodimer containing 2 similar domains and an iron-sulfur cluster.	+	'''Ferrochelatase''' (FECH) catalyzes the last step in the formation of heme. FECH adds Fe+2 to protoporphyrin IX converting it to protoheme. The human FECH is a homodimer containing 2 similar domains and an iron-sulfur cluster. '''Sirohydrochlorin ferrochelatase''' (SirB) catalyzes the addition of Fe+2 to sirohydrochlorin to produce siroheme.

	== Disease ==		== Disease ==
Line 12:		Line 12:

	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/6'>metal ions is species specific</scene>. In this way ''Bacillus subtilis'' ferrochelatase can insert copper into protoporphyrin IX, 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_zoomout/4'>Our structural work</scene> shows that <scene name='Journal:JBIC:4/Iron_binding/9'>one His residue and one Glu residue are direct ligands to the metal ion</scene>, while A third residue, Tyr in ''B. subtilis'', is a third ligand via a water molecule. Human and ''S. cerevisiae'' ferrochelatase utilizes <scene name='Journal:JBIC:4/Iron_bound_met/2'>Met as a third residue to bind the metal ligand.</scene> 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 <scene name='Journal:JBIC:4/Cobalt_bound_met_out/10'>we changed the Tyr to a Met residue</scene> and showed that the metal specificity changed so that the modified ''B. subtilis'' ferrochelatase <scene name='Journal:JBIC:4/Cobalt_bound_met/3'>preferred cobalt over copper</scene>. 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.		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/6'>metal ions is species specific</scene>. In this way ''Bacillus subtilis'' ferrochelatase can insert copper into protoporphyrin IX, 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_zoomout/4'>Our structural work</scene> shows that <scene name='Journal:JBIC:4/Iron_binding/9'>one His residue and one Glu residue are direct ligands to the metal ion</scene>, while A third residue, Tyr in ''B. subtilis'', is a third ligand via a water molecule. Human and ''S. cerevisiae'' ferrochelatase utilizes <scene name='Journal:JBIC:4/Iron_bound_met/2'>Met as a third residue to bind the metal ligand.</scene> 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 <scene name='Journal:JBIC:4/Cobalt_bound_met_out/10'>we changed the Tyr to a Met residue</scene> and showed that the metal specificity changed so that the modified ''B. subtilis'' ferrochelatase <scene name='Journal:JBIC:4/Cobalt_bound_met/3'>preferred cobalt over copper</scene>. 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.
		+
		+	==3D structures of ferrochelatase==
		+	[[Ferrochelatase 3D structures]]
		+
	</StructureSection>		</StructureSection>
-	__NOTOC__

	==3D structures of ferrochelatase==		==3D structures of ferrochelatase==
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	**[[2q2n]] – BsFECH + protoporphyrin IX + Mg<br />		**[[2q2n]] – BsFECH + protoporphyrin IX + Mg<br />
	**[[1c9e]] - BsFECH + N-methylmesoporphyrin + Cu + Mg<br />		**[[1c9e]] - BsFECH + N-methylmesoporphyrin + Cu + Mg<br />
		+
		+	* Sirohydrochlorin ferrochelatase
		+
		+	**[[5zt8]] – BsSirB <br />
		+	**[[5zt7]], [[6jv6]] – BsSirB + Co<br />
		+	**[[5zt9]] – BsSirB + Ni<br />
		+	**[[5zta]] – BsSirB + Fe<br />
	}}		}}
	== References ==		== References ==
	<references/>		<references/>
	[[Category:Topic Page]]		[[Category:Topic Page]]

Alexander Berchansky at 08:35, 6 June 2016

Alexander Berchansky — Mon, 06 Jun 2016 08:35:58 GMT

←Older revision		Revision as of 08:35, 6 June 2016
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-	<StructureSection load='1c1h' size='350' side='right' scene='' caption='Ferrochelatase with methylmesoporphyrin and Mg+2 ion (PDB code [[1c1h]])'>	+	<StructureSection load='1c1h' size='350' side='right' scene='52/526342/Cv/1' caption='Ferrochelatase with methylmesoporphyrin and Mg+2 ion (PDB code [[1c1h]])'>
	== Function ==		== Function ==

Michal Harel at 09:15, 2 March 2016

Michal Harel — Wed, 02 Mar 2016 09:15:56 GMT

←Older revision		Revision as of 09:15, 2 March 2016
Line 7:		Line 7:

	Defective FECH is the cause of erythropoietic protoporphyria (EPP), an inherited disorder of heme synthesis <ref>PMID 11929052</ref>.		Defective FECH is the cause of erythropoietic protoporphyria (EPP), an inherited disorder of heme synthesis <ref>PMID 11929052</ref>.
		+

	'''Bacterial ferrochelatase turns human: Tyr13 determines the apparent metal specificity of ''Bacillus subtilis'' ferrochelatase <ref>DOI 10.1007/s00775-010-0720-4</ref>'''		'''Bacterial ferrochelatase turns human: Tyr13 determines the apparent metal specificity of ''Bacillus subtilis'' ferrochelatase <ref>DOI 10.1007/s00775-010-0720-4</ref>'''

Michal Harel at 08:53, 2 March 2016

Michal Harel — Wed, 02 Mar 2016 08:53:04 GMT

←Older revision		Revision as of 08:53, 2 March 2016
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	== Disease ==		== Disease ==

-	Defective FECH is the cause of ~~porphyria~~<ref>PMID 11929052</ref>.	+	Defective FECH is the cause of erythropoietic protoporphyria (EPP), an inherited disorder of heme synthesis <ref>PMID 11929052</ref>.

	'''Bacterial ferrochelatase turns human: Tyr13 determines the apparent metal specificity of ''Bacillus subtilis'' ferrochelatase <ref>DOI 10.1007/s00775-010-0720-4</ref>'''		'''Bacterial ferrochelatase turns human: Tyr13 determines the apparent metal specificity of ''Bacillus subtilis'' ferrochelatase <ref>DOI 10.1007/s00775-010-0720-4</ref>'''

Michal Harel at 08:50, 2 March 2016

Michal Harel — Wed, 02 Mar 2016 08:50:15 GMT

←Older revision		Revision as of 08:50, 2 March 2016
Line 1:		Line 1:
	<StructureSection load='1c1h' size='350' side='right' scene='' caption='Ferrochelatase with methylmesoporphyrin and Mg+2 ion (PDB code [[1c1h]])'>		<StructureSection load='1c1h' size='350' side='right' scene='' caption='Ferrochelatase with methylmesoporphyrin and Mg+2 ion (PDB code [[1c1h]])'>
		+	== Function ==

-	'''Ferrochelatase''' (FECH) catalyzes the last step in the formation of heme. FECH adds Fe+2 to protoporphyrin IX converting it to protoheme. The human FECH is a homodimer containing 2 similar domains and an iron-sulfur cluster. Defective FECH is the cause of porphyria.	+	'''Ferrochelatase''' (FECH) catalyzes the last step in the formation of heme. FECH adds Fe+2 to protoporphyrin IX converting it to protoheme. The human FECH is a homodimer containing 2 similar domains and an iron-sulfur cluster.
		+
		+	== Disease ==
		+
		+	Defective FECH is the cause of porphyria<ref>PMID 11929052</ref>.

	'''Bacterial ferrochelatase turns human: Tyr13 determines the apparent metal specificity of ''Bacillus subtilis'' ferrochelatase <ref>DOI 10.1007/s00775-010-0720-4</ref>'''		'''Bacterial ferrochelatase turns human: Tyr13 determines the apparent metal specificity of ''Bacillus subtilis'' ferrochelatase <ref>DOI 10.1007/s00775-010-0720-4</ref>'''
Line 44:		Line 49:
	**[[1c9e]] - BsFECH + N-methylmesoporphyrin + Cu + Mg<br />		**[[1c9e]] - BsFECH + N-methylmesoporphyrin + Cu + Mg<br />
	}}		}}
-	~~'''~~References~~'''~~	+	== References ==
	<references/>		<references/>
	[[Category:Topic Page]]		[[Category:Topic Page]]

Michal Harel at 20:27, 21 January 2016

Michal Harel — Thu, 21 Jan 2016 20:27:39 GMT

←Older revision		Revision as of 20:27, 21 January 2016
Line 5:		Line 5:
	'''Bacterial ferrochelatase turns human: Tyr13 determines the apparent metal specificity of ''Bacillus subtilis'' ferrochelatase <ref>DOI 10.1007/s00775-010-0720-4</ref>'''		'''Bacterial ferrochelatase turns human: Tyr13 determines the apparent metal specificity of ''Bacillus subtilis'' ferrochelatase <ref>DOI 10.1007/s00775-010-0720-4</ref>'''

-	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/6'>metal ions is species specific</scene>. In this way ''Bacillus subtilis'' ferrochelatase can insert copper into protoporphyrin IX, 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_zoomout/4'>Our structural work</scene> shows that <scene name='Journal:JBIC:4/Iron_binding/9'>one His residue and one Glu residue are direct ligands to the metal ion</scene>, while A third residue, Tyr in ''B. subtilis'', is a third ligand via a water molecule. Human and ''S. cerevisiae'' ferrochelatase utilizes <scene name='Journal:JBIC:4/Iron_bound_met/2'>Met as a third residue to bind the metal ligand.</scene> 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 <scene name='Journal:JBIC:4/Cobalt_bound_met_out/10'>we changed the Tyr to a Met residue</scene> and showed that the metal specificity changed so that the modified ''B. subtilis'' ferrochelatase <scene name='Journal:JBIC:4/Cobalt_bound_met/3'>preferred cobalt over copper</scene>. 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.	+	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/6'>metal ions is species specific</scene>. In this way ''Bacillus subtilis'' ferrochelatase can insert copper into protoporphyrin IX, 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_zoomout/4'>Our structural work</scene> shows that <scene name='Journal:JBIC:4/Iron_binding/9'>one His residue and one Glu residue are direct ligands to the metal ion</scene>, while A third residue, Tyr in ''B. subtilis'', is a third ligand via a water molecule. Human and ''S. cerevisiae'' ferrochelatase utilizes <scene name='Journal:JBIC:4/Iron_bound_met/2'>Met as a third residue to bind the metal ligand.</scene> 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 <scene name='Journal:JBIC:4/Cobalt_bound_met_out/10'>we changed the Tyr to a Met residue</scene> and showed that the metal specificity changed so that the modified ''B. subtilis'' ferrochelatase <scene name='Journal:JBIC:4/Cobalt_bound_met/3'>preferred cobalt over copper</scene>. 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.
	</StructureSection>		</StructureSection>
	__NOTOC__		__NOTOC__

Michal Harel at 20:26, 21 January 2016

Michal Harel — Thu, 21 Jan 2016 20:26:25 GMT

←Older revision		Revision as of 20:26, 21 January 2016
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-	<StructureSection load='1c1h' size='~~450~~' side='right' scene='' caption='Ferrochelatase with methylmesoporphyrin and Mg+2 ion (PDB code [[1c1h]])'>	+	<StructureSection load='1c1h' size='350' side='right' scene='' caption='Ferrochelatase with methylmesoporphyrin and Mg+2 ion (PDB code [[1c1h]])'>

	'''Ferrochelatase''' (FECH) catalyzes the last step in the formation of heme. FECH adds Fe+2 to protoporphyrin IX converting it to protoheme. The human FECH is a homodimer containing 2 similar domains and an iron-sulfur cluster. Defective FECH is the cause of porphyria.		'''Ferrochelatase''' (FECH) catalyzes the last step in the formation of heme. FECH adds Fe+2 to protoporphyrin IX converting it to protoheme. The human FECH is a homodimer containing 2 similar domains and an iron-sulfur cluster. Defective FECH is the cause of porphyria.

Michal Harel at 10:47, 2 April 2015

Michal Harel — Thu, 02 Apr 2015 10:47:06 GMT

←Older revision		Revision as of 10:47, 2 April 2015
Line 35:		Line 35:

	**[[2qd3]], [[3hcn]], [[3hco]], [[3hcp]] - hFECH + protoporphyrin IX + Fe2S2<BR />		**[[2qd3]], [[3hcn]], [[3hco]], [[3hcp]] - hFECH + protoporphyrin IX + Fe2S2<BR />
		+	**[[4kla]], [[4klc]], [[4klr]], [[4kmm]] - hFECH (mutant) + protoporphyrin IX + Fe2S2<br />
	**[[3hcr]] - hFECH + protoporphyrin IX + O2 + Fe2S2<BR />		**[[3hcr]] - hFECH + protoporphyrin IX + O2 + Fe2S2<BR />
	**[[2hre]], [[2qd1]], [[2qd2]] - hFECH (mutant) + protoporphyrin IX + Fe2S2<BR />		**[[2hre]], [[2qd1]], [[2qd2]] - hFECH (mutant) + protoporphyrin IX + Fe2S2<BR />