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| - | [[Image:2po5.png|left|200px]] | |
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| - | <!-- | + | ==Crystal structure of human ferrochelatase mutant with His 263 replaced by Cys== |
| - | The line below this paragraph, containing "STRUCTURE_2po5", creates the "Structure Box" on the page.
| + | <StructureSection load='2po5' size='340' side='right'caption='[[2po5]], [[Resolution|resolution]] 2.20Å' scene=''> |
| - | You may change the PDB parameter (which sets the PDB file loaded into the applet)
| + | == Structural highlights == |
| - | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | + | <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> |
| - | or leave the SCENE parameter empty for the default display. | + | </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='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> |
| - | {{STRUCTURE_2po5| PDB=2po5 | SCENE= }}
| + | <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> |
| | + | == 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/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/main_output.php?pdb_ID=2po5 ConSurf]. |
| | + | <div style="clear:both"></div> |
| | | | |
| - | ===Crystal structure of human ferrochelatase mutant with His 263 replaced by Cys=== | + | ==See Also== |
| - | | + | *[[Ferrochelatase 3D structures|Ferrochelatase 3D structures]] |
| - | | + | == References == |
| - | <!--
| + | <references/> |
| - | The line below this paragraph, {{ABSTRACT_PUBMED_17567154}}, adds the Publication Abstract to the page
| + | __TOC__ |
| - | (as it appears on PubMed at http://www.pubmed.gov), where 17567154 is the PubMed ID number.
| + | </StructureSection> |
| - | -->
| + | |
| - | {{ABSTRACT_PUBMED_17567154}}
| + | |
| - | | + | |
| - | ==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]. | + | |
| - | | + | |
| - | ==Reference== | + | |
| - | <ref group="xtra">PMID:17567154</ref><ref group="xtra">PMID:11175906</ref><ref group="xtra">PMID:10561552</ref><references group="xtra"/> | + | |
| - | [[Category: Ferrochelatase]]
| + | |
| | [[Category: Homo sapiens]] | | [[Category: Homo sapiens]] |
| - | [[Category: Burden, A.]] | + | [[Category: Large Structures]] |
| - | [[Category: Dailey, H A.]] | + | [[Category: Burden A]] |
| - | [[Category: Dailey, T A.]] | + | [[Category: Dailey HA]] |
| - | [[Category: Horanyi, P.]] | + | [[Category: Dailey TA]] |
| - | [[Category: Medlock, A E.]] | + | [[Category: Horanyi P]] |
| - | [[Category: Najahi-Missaoui, A E.W.]] | + | [[Category: Medlock AE]] |
| - | [[Category: Rose, J P.]] | + | [[Category: Najahi-Missaoui AEW]] |
| - | [[Category: Wu, C K.]] | + | [[Category: Rose JP]] |
| - | [[Category: Fe2s2 cluster]]
| + | [[Category: Wu C-K]] |
| - | [[Category: Ferro-lyase]]
| + | |
| - | [[Category: Ferrochelatase]]
| + | |
| - | [[Category: H263c]]
| + | |
| - | [[Category: Heme biosynthesis]]
| + | |
| - | [[Category: Mature length]]
| + | |
| - | [[Category: Proteolytically processed mitochondrial inner membrane protein]]
| + | |
| - | [[Category: Protoheme]]
| + | |
| Structural highlights
Disease
HEMH_HUMAN Defects in FECH are the cause of erythropoietic protoporphyria (EPP) [MIM: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.[1] [2] [3] [4] [5] [6] [7] [8] [9] [10] [11] [12]
Function
HEMH_HUMAN Catalyzes the ferrous insertion into protoporphyrin IX.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
See Also
References
- ↑ Lamoril J, Boulechfar S, de Verneuil H, Grandchamp B, Nordmann Y, Deybach JC. Human erythropoietic protoporphyria: two point mutations in the ferrochelatase gene. Biochem Biophys Res Commun. 1991 Dec 16;181(2):594-9. PMID:1755842
- ↑ Brenner DA, Didier JM, Frasier F, Christensen SR, Evans GA, Dailey HA. A molecular defect in human protoporphyria. Am J Hum Genet. 1992 Jun;50(6):1203-10. PMID:1376018
- ↑ Sarkany RP, Alexander GJ, Cox TM. Recessive inheritance of erythropoietic protoporphyria with liver failure. Lancet. 1994 Jun 4;343(8910):1394-6. PMID:7910885
- ↑ Imoto S, Tanizawa Y, Sato Y, Kaku K, Oka Y. A novel mutation in the ferrochelatase gene associated with erythropoietic protoporphyria. Br J Haematol. 1996 Jul;94(1):191-7. PMID:8757534
- ↑ Rufenacht UB, Gouya L, Schneider-Yin X, Puy H, Schafer BW, Aquaron R, Nordmann Y, Minder EI, Deybach JC. Systematic analysis of molecular defects in the ferrochelatase gene from patients with erythropoietic protoporphyria. Am J Hum Genet. 1998 Jun;62(6):1341-52. PMID:9585598 doi:S0002-9297(07)62775-X
- ↑ Gouya L, Schneider-Yin X, Rufenacht U, Herrero C, Lecha M, Mascaro JM, Puy H, Deybach JC, Minder EI. Mutations in the ferrochelatase gene of four Spanish patients with erythropoietic protoporphyria. J Invest Dermatol. 1998 Sep;111(3):406-9. PMID:9740232 doi:10.1046/j.1523-1747.1998.00327.x
- ↑ Schneider-Yin X, Gouya L, Dorsey M, Rufenacht U, Deybach JC, Ferreira GC. Mutations in the iron-sulfur cluster ligands of the human ferrochelatase lead to erythropoietic protoporphyria. Blood. 2000 Aug 15;96(4):1545-9. PMID:10942404
- ↑ Rufenacht UB, Gregor A, Gouya L, Tarczynska-Nosal S, Schneider-Yin X, Deybach JC. New missense mutation in the human ferrochelatase gene in a family with erythropoietic protoporphyria: functional studies and correlation of genotype and phenotype. Clin Chem. 2001 Jun;47(6):1112-3. PMID:11375302
- ↑ Poh-Fitzpatrick MB, Wang X, Anderson KE, Bloomer JR, Bolwell B, Lichtin AE. Erythropoietic protoporphyria: altered phenotype after bone marrow transplantation for myelogenous leukemia in a patient heteroallelic for ferrochelatase gene mutations. J Am Acad Dermatol. 2002 Jun;46(6):861-6. PMID:12063482
- ↑ Wiman A, Floderus Y, Harper P. Novel mutations and phenotypic effect of the splice site modulator IVS3-48C in nine Swedish families with erythropoietic protoporphyria. J Hum Genet. 2003;48(2):70-6. PMID:12601550 doi:10.1007/s100380300009
- ↑ Whatley SD, Mason NG, Khan M, Zamiri M, Badminton MN, Missaoui WN, Dailey TA, Dailey HA, Douglas WS, Wainwright NJ, Elder GH. Autosomal recessive erythropoietic protoporphyria in the United Kingdom: prevalence and relationship to liver disease. J Med Genet. 2004 Aug;41(8):e105. PMID:15286165 doi:10.1136/jmg.2003.016121
- ↑ Aurizi C, Schneider-Yin X, Sorge F, Macri A, Minder EI, Biolcati G. Heterogeneity of mutations in the ferrochelatase gene in Italian patients with erythropoietic protoporphyria. Mol Genet Metab. 2007 Apr;90(4):402-7. Epub 2006 Dec 29. PMID:17196862 doi:S1096-7192(06)00355-6
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