4ivo: Difference between revisions

Latest revision as of 12:00, 1 March 2024

Structure of human protoporphyrinogen IX oxidase(R59Q)

Structural highlights

4ivo 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 2.597Å
Ligands:	ACJ, FAD, GOL
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

PPOX_HUMAN Porphyria variegata. Defects in PPOX are the cause of variegate porphyria (VP) [MIM:176200. 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. PV is the most common form of porphyria in South Africa. It is characterized by skin hyperpigmentation and hypertrichosis, abdominal pain, tachycardia, hypertension and neuromuscular disturbances. High fecal levels of protoporphyrin and coproporphyrin, increased urine uroporphyrins and iron overload are typical markers of the disease.^[1] ^[2] ^[3]

Function

PPOX_HUMAN Catalyzes the 6-electron oxidation of protoporphyrinogen-IX to form protoporphyrin-IX.

References

↑ Deybach JC, Puy H, Robreau AM, Lamoril J, Da Silva V, Grandchamp B, Nordmann Y. Mutations in the protoporphyrinogen oxidase gene in patients with variegate porphyria. Hum Mol Genet. 1996 Mar;5(3):407-10. PMID:8852667
↑ Meissner PN, Dailey TA, Hift RJ, Ziman M, Corrigall AV, Roberts AG, Meissner DM, Kirsch RE, Dailey HA. A R59W mutation in human protoporphyrinogen oxidase results in decreased enzyme activity and is prevalent in South Africans with variegate porphyria. Nat Genet. 1996 May;13(1):95-7. PMID:8673113 doi:10.1038/ng0596-95
↑ Frank J, Poh-Fitzpatrick MB, King LE Jr, Christiano AM. The genetic basis of "Scarsdale Gourmet Diet" variegate porphyria: a missense mutation in the protoporphyrinogen oxidase gene. Arch Dermatol Res. 1998 Aug;290(8):441-5. PMID:9763307

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OCA

[1] Deybach JC, Puy H, Robreau AM, Lamoril J, Da Silva V, Grandchamp B, Nordmann Y. Mutations in the protoporphyrinogen oxidase gene in patients with variegate porphyria. Hum Mol Genet. 1996 Mar;5(3):407-10. PMID:8852667

[2] Meissner PN, Dailey TA, Hift RJ, Ziman M, Corrigall AV, Roberts AG, Meissner DM, Kirsch RE, Dailey HA. A R59W mutation in human protoporphyrinogen oxidase results in decreased enzyme activity and is prevalent in South Africans with variegate porphyria. Nat Genet. 1996 May;13(1):95-7. PMID:8673113 doi:10.1038/ng0596-95

[3] Frank J, Poh-Fitzpatrick MB, King LE Jr, Christiano AM. The genetic basis of "Scarsdale Gourmet Diet" variegate porphyria: a missense mutation in the protoporphyrinogen oxidase gene. Arch Dermatol Res. 1998 Aug;290(8):441-5. PMID:9763307

[1]

[2]

[3]

@@ Line 1: / Line 1: @@
-{{STRUCTURE_4ivo|  PDB=4ivo  |  SCENE=  }}
-===Structure of human protoporphyrinogen IX oxidase(R59Q)===
-{{ABSTRACT_PUBMED_23467411}}
-==Disease==
+==Structure of human protoporphyrinogen IX oxidase(R59Q)==
-[[http://www.uniprot.org/uniprot/PPOX_HUMAN PPOX_HUMAN]] Porphyria variegata. Defects in PPOX are the cause of variegate porphyria (VP) [MIM:[http://omim.org/entry/176200 176200]]. 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. PV is the most common form of porphyria in South Africa. It is characterized by skin hyperpigmentation and hypertrichosis, abdominal pain, tachycardia, hypertension and neuromuscular disturbances. High fecal levels of protoporphyrin and coproporphyrin, increased urine uroporphyrins and iron overload are typical markers of the disease.<ref>PMID:8852667</ref> <ref>PMID:8673113</ref> <ref>PMID:9763307</ref>
+<StructureSection load='4ivo' size='340' side='right'caption='[[4ivo]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
+== Structural highlights ==
-==Function==
+<table><tr><td colspan='2'>[[4ivo]] 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=4IVO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4IVO FirstGlance]. <br>
-[[http://www.uniprot.org/uniprot/PPOX_HUMAN PPOX_HUMAN]] Catalyzes the 6-electron oxidation of protoporphyrinogen-IX to form protoporphyrin-IX.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.597&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACJ:5-[2-CHLORO-4-(TRIFLUOROMETHYL)PHENOXY]-2-NITROBENZOIC+ACID'>ACJ</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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=4ivo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ivo OCA], [https://pdbe.org/4ivo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ivo RCSB], [https://www.ebi.ac.uk/pdbsum/4ivo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ivo ProSAT]</span></td></tr>
-[[4ivo]] 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=4IVO OCA].
+</table>
+== Disease ==
-==Reference==
+[https://www.uniprot.org/uniprot/PPOX_HUMAN PPOX_HUMAN] Porphyria variegata. Defects in PPOX are the cause of variegate porphyria (VP) [MIM:[https://omim.org/entry/176200 176200]. 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. PV is the most common form of porphyria in South Africa. It is characterized by skin hyperpigmentation and hypertrichosis, abdominal pain, tachycardia, hypertension and neuromuscular disturbances. High fecal levels of protoporphyrin and coproporphyrin, increased urine uroporphyrins and iron overload are typical markers of the disease.<ref>PMID:8852667</ref> <ref>PMID:8673113</ref> <ref>PMID:9763307</ref>
-<ref group="xtra">PMID:023467411</ref><references group="xtra"/><references/>
+== Function ==
+[https://www.uniprot.org/uniprot/PPOX_HUMAN PPOX_HUMAN] Catalyzes the 6-electron oxidation of protoporphyrinogen-IX to form protoporphyrin-IX.
+== References ==
+<references/>
+__TOC__
+</StructureSection>
 [[Category: Homo sapiens]]
-[[Category: Protoporphyrinogen oxidase]]
+[[Category: Large Structures]]
-[[Category: Baifan, W.]]
+[[Category: Baifan W]]
-[[Category: Xiaohong, Q.]]
+[[Category: Xiaohong Q]]
-[[Category: Fad binding]]
-[[Category: Membrane]]
-[[Category: Oxidase]]
-[[Category: Oxidoreductase]]

4ivo: Difference between revisions

Latest revision as of 12:00, 1 March 2024

Structure of human protoporphyrinogen IX oxidase(R59Q)

Structural highlights

Disease

Function

References

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