2po5 - Revision history

OCA at 09:10, 21 February 2024

OCA — Wed, 21 Feb 2024 09:10:57 GMT

←Older revision		Revision as of 09:10, 21 February 2024
Line 3:		Line 3:
	<StructureSection load='2po5' size='340' side='right'caption='[[2po5]], [[Resolution\|resolution]] 2.20Å' scene=''>		<StructureSection load='2po5' size='340' side='right'caption='[[2po5]], [[Resolution\|resolution]] 2.20Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2po5]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PO5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PO5 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2po5]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PO5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PO5 FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=CHD:CHOLIC+ACID'>CHD</scene>~~, ~~<scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene></td></tr>~~	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 2.2Å</td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>~~[[~~Related_structure~~\|~~Related:~~]]~~</b></td><td class="sblockDat"><div style='overflow: auto~~; ~~max-height: 3em;'>[[1hrk\|1hrk]], [[2pnj\|2pnj]], [[2po7\|2po7]]</div>~~</td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CHD:CHOLIC+ACID'>CHD</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene></td></tr>
-	<tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat"~~>FECH ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&~~id=~~9606 HUMAN])</td~~><~~/tr>~~	+
-	~~<tr id~~='~~activity'><td class~~=~~"sblockLbl"><b>Activity~~:~~</b~~></td><~~td class~~=~~"sblockDat"><span class~~=~~'plainlinks~~'>~~[https://en.wikipedia.org/wiki/Ferrochelatase Ferrochelatase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.99.1.1 4.99.1.1]~~ </~~span~~></td></tr>	+
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2po5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2po5 OCA], [https://pdbe.org/2po5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2po5 RCSB], [https://www.ebi.ac.uk/pdbsum/2po5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2po5 ProSAT]</span></td></tr>		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2po5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2po5 OCA], [https://pdbe.org/2po5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2po5 RCSB], [https://www.ebi.ac.uk/pdbsum/2po5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2po5 ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[https://www.uniprot.org/uniprot/HEMH_HUMAN HEMH_HUMAN]] Defects in FECH are the cause of erythropoietic protoporphyria (EPP) [MIM:[https://omim.org/entry/177000 177000]]. Porphyrias are inherited defects in the biosynthesis of heme, resulting in the accumulation and increased excretion of porphyrins or porphyrin precursors. They are classified as erythropoietic or hepatic, depending on whether the enzyme deficiency occurs in red blood cells or in the liver. EPP is a form of porphyria marked by excessive protoporphyrin in erythrocytes, plasma, liver and feces, and by widely varying photosensitive skin changes ranging from a burning or pruritic sensation to erythema, edema and wheals.<ref>PMID:1755842</ref> <ref>PMID:1376018</ref> <ref>PMID:7910885</ref> <ref>PMID:8757534</ref> <ref>PMID:9585598</ref> <ref>PMID:9740232</ref> <ref>PMID:10942404</ref> <ref>PMID:11375302</ref> <ref>PMID:12063482</ref> <ref>PMID:12601550</ref> <ref>PMID:15286165</ref> <ref>PMID:17196862</ref>	+	[https://www.uniprot.org/uniprot/HEMH_HUMAN HEMH_HUMAN] Defects in FECH are the cause of erythropoietic protoporphyria (EPP) [MIM:[https://omim.org/entry/177000 177000]. Porphyrias are inherited defects in the biosynthesis of heme, resulting in the accumulation and increased excretion of porphyrins or porphyrin precursors. They are classified as erythropoietic or hepatic, depending on whether the enzyme deficiency occurs in red blood cells or in the liver. EPP is a form of porphyria marked by excessive protoporphyrin in erythrocytes, plasma, liver and feces, and by widely varying photosensitive skin changes ranging from a burning or pruritic sensation to erythema, edema and wheals.<ref>PMID:1755842</ref> <ref>PMID:1376018</ref> <ref>PMID:7910885</ref> <ref>PMID:8757534</ref> <ref>PMID:9585598</ref> <ref>PMID:9740232</ref> <ref>PMID:10942404</ref> <ref>PMID:11375302</ref> <ref>PMID:12063482</ref> <ref>PMID:12601550</ref> <ref>PMID:15286165</ref> <ref>PMID:17196862</ref>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/HEMH_HUMAN HEMH_HUMAN]] Catalyzes the ferrous insertion into protoporphyrin IX.	+	[https://www.uniprot.org/uniprot/HEMH_HUMAN HEMH_HUMAN] Catalyzes the ferrous insertion into protoporphyrin IX.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2po5 ConSurf].		</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2po5 ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Ferrochelatase catalyzes the terminal step in heme biosynthesis, the insertion of ferrous iron into protoporphyrin to form protoheme IX. The crystal structures of human ferrochelatase both with and without the protoporphyrin substrate bound have been determined previously. The substrate-free enzyme has an open active site pocket, while in the substrate-bound enzyme, the active site pocket is closed around the porphyrin macrocycle and a number of active site residues have reoriented side chains. To understand how and why these structural changes occur, we have substituted three amino acid residues (H263, H341, and F337) whose side chains occupy different spatial positions in the substrate-free versus substrate-bound ferrochelatases. The catalytic and structural properties of ferrochelatases containing the amino acid substitutions H263C, H341C, and F337A were examined. It was found that in the H263C and H341C variants, but not the F337A variant enzymes, the side chains of N75, M76, R164, H263, F337, H341, and E343 are oriented in a fashion similar to what is found in ferrochelatase with the bound porphyrin substrate. However, all of the variant forms possess open active site pockets which are found in the structure of porphyrin-free ferrochelatase. Thus, while the interior walls of the active site pocket are remodeled in these variants, the exterior lips remain unaltered in position. One possible explanation for this collective reorganization of active site side chains is the presence of a hydrogen bond network among H263, H341, and E343. This network is disrupted in the variants by alteration of H263C or H341C. In the substrate-bound enzyme, the formation of a hydrogen bond between H263 and a pyrrole nitrogen results in disruption of the network. The possible role of this network in catalysis is discussed.
-
-	Altered orientation of active site residues in variants of human ferrochelatase. Evidence for a hydrogen bond network involved in catalysis.,Dailey HA, Wu CK, Horanyi P, Medlock AE, Najahi-Missaoui W, Burden AE, Dailey TA, Rose J Biochemistry. 2007 Jul 10;46(27):7973-9. Epub 2007 Jun 14. PMID:17567154<ref>PMID:17567154</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 2po5" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 40:		Line 29:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Ferrochelatase]]~~	+	[[Category: Homo sapiens]]
-	~~[[Category: Human~~]]	+
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Burden, A]]	+	[[Category: Burden A]]
-	[[Category: Dailey~~, H A~~]]	+	[[Category: Dailey HA]]
-	[[Category: Dailey~~, T A~~]]	+	[[Category: Dailey TA]]
-	[[Category: Horanyi, P]]	+	[[Category: Horanyi P]]
-	[[Category: Medlock~~, A E~~]]	+	[[Category: Medlock AE]]
-	[[Category: Najahi-Missaoui~~, A E.W~~]]	+	[[Category: Najahi-Missaoui AEW]]
-	[[Category: Rose~~, J P~~]]	+	[[Category: Rose JP]]
-	[[Category: Wu, C K]]	+	[[Category: Wu C-K]]
-	~~[[Category: Fe2s2 cluster]]~~	+
-	~~[[Category: Ferro-lyase]]~~	+
-	~~[[Category: H263c]]~~	+
-	~~[[Category: Heme biosynthesis]]~~	+
-	~~[[Category: Lyase]]~~	+
-	~~[[Category: Mature length]]~~	+
-	~~[[Category: Proteolytically processed mitochondrial inner membrane protein]]~~	+
-	~~[[Category: Protoheme~~]]	+

OCA at 15:28, 17 June 2021

OCA — Thu, 17 Jun 2021 15:28:40 GMT

←Older revision		Revision as of 15:28, 17 June 2021
Line 1:		Line 1:

	==Crystal structure of human ferrochelatase mutant with His 263 replaced by Cys==		==Crystal structure of human ferrochelatase mutant with His 263 replaced by Cys==
-	<StructureSection load='2po5' size='340' side='right' caption='[[2po5]], [[Resolution\|resolution]] 2.20Å' scene=''>	+	<StructureSection load='2po5' size='340' side='right'caption='[[2po5]], [[Resolution\|resolution]] 2.20Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2po5]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PO5 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2PO5 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2po5]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PO5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PO5 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CHD:CHOLIC+ACID'>CHD</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CHD:CHOLIC+ACID'>CHD</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1hrk\|1hrk]], [[2pnj\|2pnj]], [[2po7\|2po7]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1hrk\|1hrk]], [[2pnj\|2pnj]], [[2po7\|2po7]]</div></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">FECH ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">FECH ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Ferrochelatase Ferrochelatase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.99.1.1 4.99.1.1] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Ferrochelatase Ferrochelatase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.99.1.1 4.99.1.1] </span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2po5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2po5 OCA], [~~http~~://pdbe.org/2po5 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=2po5 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/2po5 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=2po5 ProSAT]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2po5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2po5 OCA], [https://pdbe.org/2po5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2po5 RCSB], [https://www.ebi.ac.uk/pdbsum/2po5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2po5 ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[~~http~~://www.uniprot.org/uniprot/HEMH_HUMAN HEMH_HUMAN]] Defects in FECH are the cause of erythropoietic protoporphyria (EPP) [MIM:[~~http~~://omim.org/entry/177000 177000]]. Porphyrias are inherited defects in the biosynthesis of heme, resulting in the accumulation and increased excretion of porphyrins or porphyrin precursors. They are classified as erythropoietic or hepatic, depending on whether the enzyme deficiency occurs in red blood cells or in the liver. EPP is a form of porphyria marked by excessive protoporphyrin in erythrocytes, plasma, liver and feces, and by widely varying photosensitive skin changes ranging from a burning or pruritic sensation to erythema, edema and wheals.<ref>PMID:1755842</ref> <ref>PMID:1376018</ref> <ref>PMID:7910885</ref> <ref>PMID:8757534</ref> <ref>PMID:9585598</ref> <ref>PMID:9740232</ref> <ref>PMID:10942404</ref> <ref>PMID:11375302</ref> <ref>PMID:12063482</ref> <ref>PMID:12601550</ref> <ref>PMID:15286165</ref> <ref>PMID:17196862</ref>	+	[[https://www.uniprot.org/uniprot/HEMH_HUMAN HEMH_HUMAN]] Defects in FECH are the cause of erythropoietic protoporphyria (EPP) [MIM:[https://omim.org/entry/177000 177000]]. Porphyrias are inherited defects in the biosynthesis of heme, resulting in the accumulation and increased excretion of porphyrins or porphyrin precursors. They are classified as erythropoietic or hepatic, depending on whether the enzyme deficiency occurs in red blood cells or in the liver. EPP is a form of porphyria marked by excessive protoporphyrin in erythrocytes, plasma, liver and feces, and by widely varying photosensitive skin changes ranging from a burning or pruritic sensation to erythema, edema and wheals.<ref>PMID:1755842</ref> <ref>PMID:1376018</ref> <ref>PMID:7910885</ref> <ref>PMID:8757534</ref> <ref>PMID:9585598</ref> <ref>PMID:9740232</ref> <ref>PMID:10942404</ref> <ref>PMID:11375302</ref> <ref>PMID:12063482</ref> <ref>PMID:12601550</ref> <ref>PMID:15286165</ref> <ref>PMID:17196862</ref>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/HEMH_HUMAN HEMH_HUMAN]] Catalyzes the ferrous insertion into protoporphyrin IX.	+	[[https://www.uniprot.org/uniprot/HEMH_HUMAN HEMH_HUMAN]] Catalyzes the ferrous insertion into protoporphyrin IX.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/po/2po5_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/po/2po5_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
Line 33:		Line 33:
	</div>		</div>
	<div class="pdbe-citations 2po5" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 2po5" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Ferrochelatase 3D structures\|Ferrochelatase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 39:		Line 42:
	[[Category: Ferrochelatase]]		[[Category: Ferrochelatase]]
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Burden, A]]		[[Category: Burden, A]]
	[[Category: Dailey, H A]]		[[Category: Dailey, H A]]

OCA at 09:30, 18 October 2017

OCA — Wed, 18 Oct 2017 09:30:01 GMT

←Older revision		Revision as of 09:30, 18 October 2017
Line 8:		Line 8:
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">FECH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">FECH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ferrochelatase Ferrochelatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.99.1.1 4.99.1.1] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ferrochelatase Ferrochelatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.99.1.1 4.99.1.1] </span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2po5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2po5 OCA], [http://pdbe.org/2po5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2po5 RCSB], [http://www.ebi.ac.uk/pdbsum/2po5 PDBsum]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2po5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2po5 OCA], [http://pdbe.org/2po5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2po5 RCSB], [http://www.ebi.ac.uk/pdbsum/2po5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2po5 ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 33:		Line 33:
	</div>		</div>
	<div class="pdbe-citations 2po5" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 2po5" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Ferrochelatase\|Ferrochelatase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 10:21, 26 February 2016

OCA — Fri, 26 Feb 2016 10:21:39 GMT

←Older revision		Revision as of 10:21, 26 February 2016
Line 1:		Line 1:
		+
	==Crystal structure of human ferrochelatase mutant with His 263 replaced by Cys==		==Crystal structure of human ferrochelatase mutant with His 263 replaced by Cys==
	<StructureSection load='2po5' size='340' side='right' caption='[[2po5]], [[Resolution\|resolution]] 2.20Å' scene=''>		<StructureSection load='2po5' size='340' side='right' caption='[[2po5]], [[Resolution\|resolution]] 2.20Å' scene=''>

OCA at 02:19, 9 February 2016

OCA — Tue, 09 Feb 2016 02:19:59 GMT

←Older revision		Revision as of 02:19, 9 February 2016
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	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</jmolCheckbox>
-	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/~~chain_selection~~.php?pdb_ID=~~2ata~~ ConSurf].	+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2po5 ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 17:39, 10 September 2015

OCA — Thu, 10 Sep 2015 17:39:31 GMT

←Older revision		Revision as of 17:39, 10 September 2015
Line 2:		Line 2:
	<StructureSection load='2po5' size='340' side='right' caption='[[2po5]], [[Resolution\|resolution]] 2.20Å' scene=''>		<StructureSection load='2po5' size='340' side='right' caption='[[2po5]], [[Resolution\|resolution]] 2.20Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2po5]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Homo_sapiens Homo sapiens~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PO5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2PO5 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2po5]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PO5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2PO5 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CHD:CHOLIC+ACID'>CHD</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CHD:CHOLIC+ACID'>CHD</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1hrk\|1hrk]], [[2pnj\|2pnj]], [[2po7\|2po7]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1hrk\|1hrk]], [[2pnj\|2pnj]], [[2po7\|2po7]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">FECH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 ~~Homo sapiens~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">FECH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ferrochelatase Ferrochelatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.99.1.1 4.99.1.1] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ferrochelatase Ferrochelatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.99.1.1 4.99.1.1] </span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2po5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2po5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2po5 RCSB], [http://www.ebi.ac.uk/pdbsum/2po5 PDBsum]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2po5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2po5 OCA], [http://pdbe.org/2po5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2po5 RCSB], [http://www.ebi.ac.uk/pdbsum/2po5 PDBsum]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 31:		Line 31:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 2po5" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 39:		Line 40:
	</StructureSection>		</StructureSection>
	[[Category: Ferrochelatase]]		[[Category: Ferrochelatase]]
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Burden, A]]		[[Category: Burden, A]]
	[[Category: Dailey, H A]]		[[Category: Dailey, H A]]

OCA at 16:19, 19 January 2015

OCA — Mon, 19 Jan 2015 16:19:58 GMT

←Older revision		Revision as of 16:19, 19 January 2015
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2po5]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PO5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2PO5 FirstGlance]. <br>		<table><tr><td colspan='2'>[[2po5]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PO5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2PO5 FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CHD:CHOLIC+ACID'>CHD</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CHD:CHOLIC+ACID'>CHD</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1hrk\|1hrk]], [[2pnj\|2pnj]], [[2po7\|2po7]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1hrk\|1hrk]], [[2pnj\|2pnj]], [[2po7\|2po7]]</td></tr>
-	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">FECH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">FECH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ferrochelatase Ferrochelatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.99.1.1 4.99.1.1] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ferrochelatase Ferrochelatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.99.1.1 4.99.1.1] </span></td></tr>
-	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2po5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2po5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2po5 RCSB], [http://www.ebi.ac.uk/pdbsum/2po5 PDBsum]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2po5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2po5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2po5 RCSB], [http://www.ebi.ac.uk/pdbsum/2po5 PDBsum]</span></td></tr>
-	<table>	+	</table>
	== Disease ==		== Disease ==
	[[http://www.uniprot.org/uniprot/HEMH_HUMAN HEMH_HUMAN]] Defects in FECH are the cause of erythropoietic protoporphyria (EPP) [MIM:[http://omim.org/entry/177000 177000]]. Porphyrias are inherited defects in the biosynthesis of heme, resulting in the accumulation and increased excretion of porphyrins or porphyrin precursors. They are classified as erythropoietic or hepatic, depending on whether the enzyme deficiency occurs in red blood cells or in the liver. EPP is a form of porphyria marked by excessive protoporphyrin in erythrocytes, plasma, liver and feces, and by widely varying photosensitive skin changes ranging from a burning or pruritic sensation to erythema, edema and wheals.<ref>PMID:1755842</ref> <ref>PMID:1376018</ref> <ref>PMID:7910885</ref> <ref>PMID:8757534</ref> <ref>PMID:9585598</ref> <ref>PMID:9740232</ref> <ref>PMID:10942404</ref> <ref>PMID:11375302</ref> <ref>PMID:12063482</ref> <ref>PMID:12601550</ref> <ref>PMID:15286165</ref> <ref>PMID:17196862</ref>		[[http://www.uniprot.org/uniprot/HEMH_HUMAN HEMH_HUMAN]] Defects in FECH are the cause of erythropoietic protoporphyria (EPP) [MIM:[http://omim.org/entry/177000 177000]]. Porphyrias are inherited defects in the biosynthesis of heme, resulting in the accumulation and increased excretion of porphyrins or porphyrin precursors. They are classified as erythropoietic or hepatic, depending on whether the enzyme deficiency occurs in red blood cells or in the liver. EPP is a form of porphyria marked by excessive protoporphyrin in erythrocytes, plasma, liver and feces, and by widely varying photosensitive skin changes ranging from a burning or pruritic sensation to erythema, edema and wheals.<ref>PMID:1755842</ref> <ref>PMID:1376018</ref> <ref>PMID:7910885</ref> <ref>PMID:8757534</ref> <ref>PMID:9585598</ref> <ref>PMID:9740232</ref> <ref>PMID:10942404</ref> <ref>PMID:11375302</ref> <ref>PMID:12063482</ref> <ref>PMID:12601550</ref> <ref>PMID:15286165</ref> <ref>PMID:17196862</ref>
Line 40:		Line 40:
	[[Category: Ferrochelatase]]		[[Category: Ferrochelatase]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
-	[[Category: Burden, A.]]	+	[[Category: Burden, A]]
-	[[Category: Dailey, H A.]]	+	[[Category: Dailey, H A]]
-	[[Category: Dailey, T A.]]	+	[[Category: Dailey, T A]]
-	[[Category: Horanyi, P.]]	+	[[Category: Horanyi, P]]
-	[[Category: Medlock, A E.]]	+	[[Category: Medlock, A E]]
-	[[Category: Najahi-Missaoui, A E.W.]]	+	[[Category: Najahi-Missaoui, A E.W]]
-	[[Category: Rose, J P.]]	+	[[Category: Rose, J P]]
-	[[Category: Wu, C K.]]	+	[[Category: Wu, C K]]
	[[Category: Fe2s2 cluster]]		[[Category: Fe2s2 cluster]]
	[[Category: Ferro-lyase]]		[[Category: Ferro-lyase]]
-	[[Category: Ferrochelatase]]
	[[Category: H263c]]		[[Category: H263c]]
	[[Category: Heme biosynthesis]]		[[Category: Heme biosynthesis]]

OCA at 19:14, 30 September 2014

OCA — Tue, 30 Sep 2014 19:14:54 GMT

←Older revision		Revision as of 19:14, 30 September 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_2po5\| PDB=2po5 \| SCENE= }}~~	+	==Crystal structure of human ferrochelatase mutant with His 263 replaced by Cys==
-	===Crystal structure of human ferrochelatase mutant with His 263 replaced by Cys===	+	<StructureSection load='2po5' size='340' side='right' caption='[[2po5]], [[Resolution\|resolution]] 2.20Å' scene=''>
-	~~{{ABSTRACT_PUBMED_17567154}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[2po5]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PO5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2PO5 FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CHD:CHOLIC+ACID'>CHD</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1hrk\|1hrk]], [[2pnj\|2pnj]], [[2po7\|2po7]]</td></tr>
		+	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">FECH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ferrochelatase Ferrochelatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.99.1.1 4.99.1.1] </span></td></tr>
		+	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2po5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2po5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2po5 RCSB], [http://www.ebi.ac.uk/pdbsum/2po5 PDBsum]</span></td></tr>
		+	<table>
		+	== Disease ==
		+	[[http://www.uniprot.org/uniprot/HEMH_HUMAN HEMH_HUMAN]] Defects in FECH are the cause of erythropoietic protoporphyria (EPP) [MIM:[http://omim.org/entry/177000 177000]]. Porphyrias are inherited defects in the biosynthesis of heme, resulting in the accumulation and increased excretion of porphyrins or porphyrin precursors. They are classified as erythropoietic or hepatic, depending on whether the enzyme deficiency occurs in red blood cells or in the liver. EPP is a form of porphyria marked by excessive protoporphyrin in erythrocytes, plasma, liver and feces, and by widely varying photosensitive skin changes ranging from a burning or pruritic sensation to erythema, edema and wheals.<ref>PMID:1755842</ref> <ref>PMID:1376018</ref> <ref>PMID:7910885</ref> <ref>PMID:8757534</ref> <ref>PMID:9585598</ref> <ref>PMID:9740232</ref> <ref>PMID:10942404</ref> <ref>PMID:11375302</ref> <ref>PMID:12063482</ref> <ref>PMID:12601550</ref> <ref>PMID:15286165</ref> <ref>PMID:17196862</ref>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/HEMH_HUMAN HEMH_HUMAN]] Catalyzes the ferrous insertion into protoporphyrin IX.
		+	== Evolutionary Conservation ==
		+	[[Image:Consurf_key_small.gif\|200px\|right]]
		+	Check<jmol>
		+	<jmolCheckbox>
		+	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/po/2po5_consurf.spt"</scriptWhenChecked>
		+	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
		+	<text>to colour the structure by Evolutionary Conservation</text>
		+	</jmolCheckbox>
		+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
		+	<div style="clear:both"></div>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Ferrochelatase catalyzes the terminal step in heme biosynthesis, the insertion of ferrous iron into protoporphyrin to form protoheme IX. The crystal structures of human ferrochelatase both with and without the protoporphyrin substrate bound have been determined previously. The substrate-free enzyme has an open active site pocket, while in the substrate-bound enzyme, the active site pocket is closed around the porphyrin macrocycle and a number of active site residues have reoriented side chains. To understand how and why these structural changes occur, we have substituted three amino acid residues (H263, H341, and F337) whose side chains occupy different spatial positions in the substrate-free versus substrate-bound ferrochelatases. The catalytic and structural properties of ferrochelatases containing the amino acid substitutions H263C, H341C, and F337A were examined. It was found that in the H263C and H341C variants, but not the F337A variant enzymes, the side chains of N75, M76, R164, H263, F337, H341, and E343 are oriented in a fashion similar to what is found in ferrochelatase with the bound porphyrin substrate. However, all of the variant forms possess open active site pockets which are found in the structure of porphyrin-free ferrochelatase. Thus, while the interior walls of the active site pocket are remodeled in these variants, the exterior lips remain unaltered in position. One possible explanation for this collective reorganization of active site side chains is the presence of a hydrogen bond network among H263, H341, and E343. This network is disrupted in the variants by alteration of H263C or H341C. In the substrate-bound enzyme, the formation of a hydrogen bond between H263 and a pyrrole nitrogen results in disruption of the network. The possible role of this network in catalysis is discussed.

-	~~==Disease==~~	+	Altered orientation of active site residues in variants of human ferrochelatase. Evidence for a hydrogen bond network involved in catalysis.,Dailey HA, Wu CK, Horanyi P, Medlock AE, Najahi-Missaoui W, Burden AE, Dailey TA, Rose J Biochemistry. 2007 Jul 10;46(27):7973-9. Epub 2007 Jun 14. PMID:17567154<ref>PMID:17567154</ref>
-	~~[[http://www.uniprot.org/uniprot/HEMH_HUMAN HEMH_HUMAN]] Defects in FECH are the cause~~ of ~~erythropoietic protoporphyria (EPP) [MIM:[http://omim.org/entry/177000 177000]]. Porphyrias are inherited defects~~ in ~~the biosynthesis~~ of ~~heme, resulting in the accumulation and increased excretion of porphyrins or porphyrin precursors~~. ~~They are classified as erythropoietic or hepatic, depending on whether the enzyme deficiency occurs~~ in ~~red blood cells or in the liver~~. ~~EPP is a form of porphyria marked by excessive protoporphyrin in erythrocytes~~, ~~plasma~~, ~~liver and feces~~, ~~and by widely varying photosensitive skin changes ranging from a burning or pruritic sensation to erythema~~, ~~edema and wheals~~.~~<ref>PMID~~:~~1755842</ref><ref>~~PMID:1376018</ref><ref>PMID:7910885</ref><ref>PMID:8757534</ref><ref>PMID:9585598</ref><ref>PMID:9740232</ref><ref>PMID:10942404</ref><ref>PMID:11375302</ref><ref>PMID:12063482</ref><ref>PMID:12601550</ref><ref>PMID:15286165</ref><ref>PMID:~~17196862~~</ref>	+

-	~~==Function==~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[http:~~/~~/www~~.~~uniprot~~.~~org/uniprot/HEMH_HUMAN HEMH_HUMAN]] Catalyzes the ferrous insertion into protoporphyrin IX~~.	+	</div>
-		+
-	~~==About this Structure==~~	+
-	~~[[2po5]] is a 2 chain structure with sequence from [http:~~/~~/en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PO5 OCA].~~	+

	==See Also==		==See Also==
	*[[Ferrochelatase\|Ferrochelatase]]		*[[Ferrochelatase\|Ferrochelatase]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	~~<ref group="xtra">PMID:017567154</ref><ref group="xtra">PMID:011175906</ref><ref group="xtra">PMID:010561552</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Ferrochelatase]]		[[Category: Ferrochelatase]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]

OCA at 01:06, 25 March 2013

OCA — Mon, 25 Mar 2013 01:06:19 GMT

←Older revision		Revision as of 01:06, 25 March 2013
Line 1:		Line 1:
-	[[Image:2po5.png\|left\|200px]]
-
	{{STRUCTURE_2po5\| PDB=2po5 \| SCENE= }}		{{STRUCTURE_2po5\| PDB=2po5 \| SCENE= }}
-
	===Crystal structure of human ferrochelatase mutant with His 263 replaced by Cys===		===Crystal structure of human ferrochelatase mutant with His 263 replaced by Cys===
		+	{{ABSTRACT_PUBMED_17567154}}

-	~~{{ABSTRACT_PUBMED_17567154}}~~	+	==Disease==
		+	[[http://www.uniprot.org/uniprot/HEMH_HUMAN HEMH_HUMAN]] Defects in FECH are the cause of erythropoietic protoporphyria (EPP) [MIM:[http://omim.org/entry/177000 177000]]. Porphyrias are inherited defects in the biosynthesis of heme, resulting in the accumulation and increased excretion of porphyrins or porphyrin precursors. They are classified as erythropoietic or hepatic, depending on whether the enzyme deficiency occurs in red blood cells or in the liver. EPP is a form of porphyria marked by excessive protoporphyrin in erythrocytes, plasma, liver and feces, and by widely varying photosensitive skin changes ranging from a burning or pruritic sensation to erythema, edema and wheals.<ref>PMID:1755842</ref><ref>PMID:1376018</ref><ref>PMID:7910885</ref><ref>PMID:8757534</ref><ref>PMID:9585598</ref><ref>PMID:9740232</ref><ref>PMID:10942404</ref><ref>PMID:11375302</ref><ref>PMID:12063482</ref><ref>PMID:12601550</ref><ref>PMID:15286165</ref><ref>PMID:17196862</ref>
		+
		+	==Function==
		+	[[http://www.uniprot.org/uniprot/HEMH_HUMAN HEMH_HUMAN]] Catalyzes the ferrous insertion into protoporphyrin IX.

	==About this Structure==		==About this Structure==
Line 14:		Line 16:

	==Reference==		==Reference==
-	<ref group="xtra">PMID:017567154</ref><ref group="xtra">PMID:011175906</ref><ref group="xtra">PMID:010561552</ref><references group="xtra"/>	+	<ref group="xtra">PMID:017567154</ref><ref group="xtra">PMID:011175906</ref><ref group="xtra">PMID:010561552</ref><references group="xtra"/><references/>
	[[Category: Ferrochelatase]]		[[Category: Ferrochelatase]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]

OCA at 13:03, 30 January 2013

OCA — Wed, 30 Jan 2013 13:03:14 GMT

←Older revision		Revision as of 13:03, 30 January 2013
Line 1:		Line 1:
	[[Image:2po5.png\|left\|200px]]		[[Image:2po5.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_2po5", creates the "Structure Box" on the page.
-	You may change the PDB parameter (which sets the PDB file loaded into the applet)
-	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-	or leave the SCENE parameter empty for the default display.
-	-->
	{{STRUCTURE_2po5\| PDB=2po5 \| SCENE= }}		{{STRUCTURE_2po5\| PDB=2po5 \| SCENE= }}

	===Crystal structure of human ferrochelatase mutant with His 263 replaced by Cys===		===Crystal structure of human ferrochelatase mutant with His 263 replaced by Cys===

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	==About this Structure==		==About this Structure==
	[[2po5]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PO5 OCA].		[[2po5]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PO5 OCA].
		+
		+	==See Also==
		+	*[[Ferrochelatase\|Ferrochelatase]]

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~17567154~~</ref><ref group="xtra">PMID:~~11175906~~</ref><ref group="xtra">PMID:~~10561552~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:017567154</ref><ref group="xtra">PMID:011175906</ref><ref group="xtra">PMID:010561552</ref><references group="xtra"/>
	[[Category: Ferrochelatase]]		[[Category: Ferrochelatase]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
Line 38:		Line 30:
	[[Category: H263c]]		[[Category: H263c]]
	[[Category: Heme biosynthesis]]		[[Category: Heme biosynthesis]]
		+	[[Category: Lyase]]
	[[Category: Mature length]]		[[Category: Mature length]]
	[[Category: Proteolytically processed mitochondrial inner membrane protein]]		[[Category: Proteolytically processed mitochondrial inner membrane protein]]
	[[Category: Protoheme]]		[[Category: Protoheme]]