2qd1

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{{Seed}}
 
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[[Image:2qd1.png|left|200px]]
 
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==2.2 Angstrom Structure of the human ferrochelatase variant E343K with substrate bound==
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The line below this paragraph, containing "STRUCTURE_2qd1", creates the "Structure Box" on the page.
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<StructureSection load='2qd1' size='340' side='right'caption='[[2qd1]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2qd1]] is a 4 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=2QD1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2QD1 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
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<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>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=PP9:PROTOPORPHYRIN+IX'>PP9</scene></td></tr>
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{{STRUCTURE_2qd1| PDB=2qd1 | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2qd1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qd1 OCA], [https://pdbe.org/2qd1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2qd1 RCSB], [https://www.ebi.ac.uk/pdbsum/2qd1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2qd1 ProSAT]</span></td></tr>
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</table>
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== Disease ==
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[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>
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== Function ==
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[https://www.uniprot.org/uniprot/HEMH_HUMAN HEMH_HUMAN] Catalyzes the ferrous insertion into protoporphyrin IX.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qd/2qd1_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=2qd1 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Ferrochelatase (protoheme ferrolyase, EC 4.99.1.1) is the terminal enzyme in heme biosynthesis and catalyzes the insertion of ferrous iron into protoporphyrin IX to form protoheme IX (heme). Due to the many critical roles of heme, synthesis of heme is required by the vast majority of organisms. Despite significant investigation of both the microbial and eukaryotic enzyme, details of metal chelation remain unidentified. Here we present the first structure of the wild-type human enzyme, a lead-inhibited intermediate of the wild-type enzyme with bound metallated porphyrin macrocycle, the product bound form of the enzyme, and a higher resolution model for the substrate-bound form of the E343K variant. These data paint a picture of an enzyme that undergoes significant changes in secondary structure during the catalytic cycle. The role that these structural alterations play in overall catalysis and potential protein-protein interactions with other proteins, as well as the possible molecular basis for these changes, is discussed. The atomic details and structural rearrangements presented herein significantly advance our understanding of the substrate binding mode of ferrochelatase and reveal new conformational changes in a structurally conserved pi-helix that is predicted to have a central role in product release.
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===2.2 Angstrom Structure of the human ferrochelatase variant E343K with substrate bound===
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A pi-helix switch selective for porphyrin deprotonation and product release in human ferrochelatase.,Medlock AE, Dailey TA, Ross TA, Dailey HA, Lanzilotta WN J Mol Biol. 2007 Nov 2;373(4):1006-16. Epub 2007 Aug 23. PMID:17884090<ref>PMID:17884090</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2qd1" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_17884090}}, adds the Publication Abstract to the page
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*[[Ferrochelatase 3D structures|Ferrochelatase 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 17884090 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_17884090}}
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__TOC__
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</StructureSection>
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==Disease==
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Known disease associated with this structure: Protoporphyria, erythropoietic, autosomal dominant OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=612386 612386]], Protoporphyria, erythropoietic, autosomal recessive OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=612386 612386]]
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==About this Structure==
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2QD1 is a 4 chains structure of sequences 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=2QD1 OCA].
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==Reference==
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<ref group="xtra">PMID:17884090</ref><references group="xtra"/>
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[[Category: Ferrochelatase]]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Dailey, H A.]]
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[[Category: Large Structures]]
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[[Category: Dailey, T A.]]
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[[Category: Dailey HA]]
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[[Category: Lanzilotta, W N.]]
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[[Category: Dailey TA]]
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[[Category: Medlock, A E.]]
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[[Category: Lanzilotta WN]]
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[[Category: Ross, T A.]]
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[[Category: Medlock AE]]
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[[Category: Ferrochelatase]]
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[[Category: Ross TA]]
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[[Category: Heme biosynthesis]]
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[[Category: Lyase]]
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[[Category: Protopophyrin ix]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 16:17:28 2009''
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Current revision

2.2 Angstrom Structure of the human ferrochelatase variant E343K with substrate bound

PDB ID 2qd1

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