View source for 1hrk


==CRYSTAL STRUCTURE OF HUMAN FERROCHELATASE==
<StructureSection load='1hrk' size='340' side='right'caption='[[1hrk]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1hrk]] 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=1HRK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HRK 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>
<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=1hrk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hrk OCA], [https://pdbe.org/1hrk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hrk RCSB], [https://www.ebi.ac.uk/pdbsum/1hrk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hrk ProSAT]</span></td></tr>
</table>
== 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>  
== Function ==
[[https://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/hr/1hrk_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/main_output.php?pdb_ID=1hrk ConSurf].
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== Publication Abstract from PubMed ==
Human ferrochelatase (E.C. 4.99.1.1) is a homodimeric (86 kDa) mitochondrial membrane-associated enzyme that catalyzes the insertion of ferrous iron into protoporphyrin to form heme. We have determined the 2.0 A structure from the single wavelength iron anomalous scattering signal. The enzyme contains two NO-sensitive and uniquely coordinated [2Fe-2S] clusters. Its membrane association is mediated in part by a 12-residue hydrophobic lip that also forms the entrance to the active site pocket. The positioning of highly conserved residues in the active site in conjunction with previous biochemical studies support a catalytic model that may have significance in explaining the enzymatic defects that lead to the human inherited disease erythropoietic protoporphyria.

The 2.0 A structure of human ferrochelatase, the terminal enzyme of heme biosynthesis.,Wu CK, Dailey HA, Rose JP, Burden A, Sellers VM, Wang BC Nat Struct Biol. 2001 Feb;8(2):156-60. PMID:11175906<ref>PMID:11175906</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 1hrk" style="background-color:#fffaf0;"></div>

==See Also==
*[[Ferrochelatase 3D structures|Ferrochelatase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Ferrochelatase]]
[[Category: Human]]
[[Category: Large Structures]]
[[Category: Burden, A]]
[[Category: Dailey, H A]]
[[Category: Rose, J P]]
[[Category: Sellers, V M]]
[[Category: Wang, B C]]
[[Category: Wu, C K]]
[[Category: Fe2s2 cluster]]
[[Category: Heme biosynthesis]]
[[Category: Lyase]]
[[Category: Mature length]]
[[Category: Proteolytically processed mitochondrial inner membrane protein]]
[[Category: Protoheme ferro-lyase]]