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[[Image:2aex.png|left|200px]]


{{STRUCTURE_2aex|  PDB=2aex  |  SCENE=  }}
==The 1.58A Crystal Structure of Human Coproporphyrinogen Oxidase Reveals the Structural Basis of Hereditary Coproporphyria==
 
<StructureSection load='2aex' size='340' side='right'caption='[[2aex]], [[Resolution|resolution]] 1.58&Aring;' scene=''>
===The 1.58A Crystal Structure of Human Coproporphyrinogen Oxidase Reveals the Structural Basis of Hereditary Coproporphyria===
== Structural highlights ==
 
<table><tr><td colspan='2'>[[2aex]] is a 1 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=2AEX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2AEX FirstGlance]. <br>
{{ABSTRACT_PUBMED_16176984}}
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.58&#8491;</td></tr>
 
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene></td></tr>
==About this Structure==
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2aex FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2aex OCA], [https://pdbe.org/2aex PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2aex RCSB], [https://www.ebi.ac.uk/pdbsum/2aex PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2aex ProSAT]</span></td></tr>
[[2aex]] is a 1 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=2AEX OCA].  
</table>
 
== Disease ==
==Reference==
[https://www.uniprot.org/uniprot/HEM6_HUMAN HEM6_HUMAN] Defects in CPOX are the cause of hereditary coproporphyria (HCP) [MIM:[https://omim.org/entry/121300 121300]. HCP is an acute hepatic porphyria and an autosomal dominant disease characterized by neuropsychiatric disturbances and skin photosensitivity. Biochemically, there is an overexcretion of coproporphyrin III in the urine and in the feces. HCP is clinically characterized by attacks of abdominal pain, neurological disturbances, and psychiatric symptoms. The symptoms are generally manifested with rapid onset, and can be precipitated by drugs, alcohol, caloric deprivation, infection, endocrine factors or stress. A severe variant form is harderoporphyria, which is characterized by earlier onset attacks, massive excretion of harderoporphyrin in the feces, and a marked decrease of coproporphyrinogen IX oxidase activity.<ref>PMID:8012360</ref> <ref>PMID:7849704</ref> <ref>PMID:7757079</ref> <ref>PMID:9048920</ref> <ref>PMID:8990017</ref> <ref>PMID:9298818</ref> <ref>PMID:9888388</ref> <ref>PMID:12181641</ref> <ref>PMID:15896662</ref> <ref>PMID:16398658</ref>
<ref group="xtra">PMID:016176984</ref><references group="xtra"/>
== Function ==
[[Category: Coproporphyrinogen oxidase]]
[https://www.uniprot.org/uniprot/HEM6_HUMAN HEM6_HUMAN] Key enzyme in heme biosynthesis. Catalyzes the oxidative decarboxylation of propionic acid side chains of rings A and B of coproporphyrinogen III.
== 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/ae/2aex_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=2aex ConSurf].
<div style="clear:both"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Bodnarova, M.]]
[[Category: Large Structures]]
[[Category: Demeler, B.]]
[[Category: Bodnarova M]]
[[Category: Flachsova, E.]]
[[Category: Demeler B]]
[[Category: Lee, D S.]]
[[Category: Flachsova E]]
[[Category: Martasek, P.]]
[[Category: Lee DS]]
[[Category: Raman, C S.]]
[[Category: Martasek P]]
[[Category: Flat beta-sheet sandwiched by helice]]
[[Category: Raman CS]]
[[Category: Oxidoreductase]]

Latest revision as of 12:12, 14 February 2024

The 1.58A Crystal Structure of Human Coproporphyrinogen Oxidase Reveals the Structural Basis of Hereditary CoproporphyriaThe 1.58A Crystal Structure of Human Coproporphyrinogen Oxidase Reveals the Structural Basis of Hereditary Coproporphyria

Structural highlights

2aex is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.58Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

HEM6_HUMAN Defects in CPOX are the cause of hereditary coproporphyria (HCP) [MIM:121300. HCP is an acute hepatic porphyria and an autosomal dominant disease characterized by neuropsychiatric disturbances and skin photosensitivity. Biochemically, there is an overexcretion of coproporphyrin III in the urine and in the feces. HCP is clinically characterized by attacks of abdominal pain, neurological disturbances, and psychiatric symptoms. The symptoms are generally manifested with rapid onset, and can be precipitated by drugs, alcohol, caloric deprivation, infection, endocrine factors or stress. A severe variant form is harderoporphyria, which is characterized by earlier onset attacks, massive excretion of harderoporphyrin in the feces, and a marked decrease of coproporphyrinogen IX oxidase activity.[1] [2] [3] [4] [5] [6] [7] [8] [9] [10]

Function

HEM6_HUMAN Key enzyme in heme biosynthesis. Catalyzes the oxidative decarboxylation of propionic acid side chains of rings A and B of coproporphyrinogen III.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

References

  1. ↑ Martasek P, Nordmann Y, Grandchamp B. Homozygous hereditary coproporphyria caused by an arginine to tryptophane substitution in coproporphyrinogen oxidase and common intragenic polymorphisms. Hum Mol Genet. 1994 Mar;3(3):477-80. PMID:8012360
  2. ↑ Fujita H, Kondo M, Taketani S, Nomura N, Furuyama K, Akagi R, Nagai T, Terajima M, Galbraith RA, Sassa S. Characterization and expression of cDNA encoding coproporphyrinogen oxidase from a patient with hereditary coproporphyria. Hum Mol Genet. 1994 Oct;3(10):1807-10. PMID:7849704
  3. ↑ Lamoril J, Martasek P, Deybach JC, Da Silva V, Grandchamp B, Nordmann Y. A molecular defect in coproporphyrinogen oxidase gene causing harderoporphyria, a variant form of hereditary coproporphyria. Hum Mol Genet. 1995 Feb;4(2):275-8. PMID:7757079
  4. ↑ Daimon M, Gojyou E, Sugawara M, Yamatani K, Tominaga M, Sasaki H. A novel missense mutation in exon 4 of the human coproporphyrinogen oxidase gene in two patients with hereditary coproporphyria. Hum Genet. 1997 Feb;99(2):199-201. PMID:9048920
  5. ↑ Lamoril J, Deybach JC, Puy H, Grandchamp B, Nordmann Y. Three novel mutations in the coproporphyrinogen oxidase gene. Hum Mutat. 1997;9(1):78-80. PMID:8990017 doi:<78::AID-HUMU17>3.0.CO;2-M 10.1002/(SICI)1098-1004(1997)9:1<78::AID-HUMU17>3.0.CO;2-M
  6. ↑ Schreiber WE, Zhang X, Senz J, Jamani A. Hereditary coproporphyria: exon screening by heteroduplex analysis detects three novel mutations in the coproporphyrinogen oxidase gene. Hum Mutat. 1997;10(3):196-200. PMID:9298818 doi:<196::AID-HUMU3>3.0.CO;2-H 10.1002/(SICI)1098-1004(1997)10:3<196::AID-HUMU3>3.0.CO;2-H
  7. ↑ Rosipal R, Lamoril J, Puy H, Da Silva V, Gouya L, De Rooij FW, Te Velde K, Nordmann Y, Martasek P, Deybach JC. Systematic analysis of coproporphyrinogen oxidase gene defects in hereditary coproporphyria and mutation update. Hum Mutat. 1999;13(1):44-53. PMID:9888388 doi:<44::AID-HUMU5>3.0.CO;2-Q 10.1002/(SICI)1098-1004(1999)13:1<44::AID-HUMU5>3.0.CO;2-Q
  8. ↑ Wiman A, Floderus Y, Harper P. Two novel mutations and coexistence of the 991C>T and the 1339C>T mutation on a single allele in the coproporphyrinogen oxidase gene in Swedish patients with hereditary coproporphyria. J Hum Genet. 2002;47(8):407-12. PMID:12181641 doi:10.1007/s100380200059
  9. ↑ To-Figueras J, Badenas C, Enriquez MT, Segura S, Alvarez C, Mila M, Lecha M, Herrero C. Biochemical and genetic characterization of four cases of hereditary coproporphyria in Spain. Mol Genet Metab. 2005 Jun;85(2):160-3. Epub 2005 Feb 25. PMID:15896662 doi:10.1016/j.ymgme.2004.12.012
  10. ↑ Akagi R, Inoue R, Muranaka S, Tahara T, Taketani S, Anderson KE, Phillips JD, Sassa S. Dual gene defects involving delta-aminolaevulinate dehydratase and coproporphyrinogen oxidase in a porphyria patient. Br J Haematol. 2006 Jan;132(2):237-43. PMID:16398658 doi:10.1111/j.1365-2141.2005.05852.x

2aex, resolution 1.58Å

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