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| <StructureSection load='1p49' size='340' side='right'caption='[[1p49]], [[Resolution|resolution]] 2.60Å' scene=''> | | <StructureSection load='1p49' size='340' side='right'caption='[[1p49]], [[Resolution|resolution]] 2.60Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[1p49]] 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=1P49 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1P49 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1p49]] 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=1P49 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1P49 FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BOG:B-OCTYLGLUCOSIDE'>BOG</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6Å</td></tr> |
- | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ALS:(3S)-3-(SULFOOXY)-L-SERINE'>ALS</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ALS:(3S)-3-(SULFOOXY)-L-SERINE'>ALS</scene>, <scene name='pdbligand=BOG:B-OCTYLGLUCOSIDE'>BOG</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> |
- | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Steryl-sulfatase Steryl-sulfatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.6.2 3.1.6.2] </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=1p49 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p49 OCA], [https://pdbe.org/1p49 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1p49 RCSB], [https://www.ebi.ac.uk/pdbsum/1p49 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1p49 ProSAT]</span></td></tr> |
- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1p49 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p49 OCA], [http://pdbe.org/1p49 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1p49 RCSB], [http://www.ebi.ac.uk/pdbsum/1p49 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1p49 ProSAT]</span></td></tr> | + | |
| </table> | | </table> |
| == Disease == | | == Disease == |
- | [[http://www.uniprot.org/uniprot/STS_HUMAN STS_HUMAN]] Defects in STS are the cause of ichthyosis X-linked (IXL) [MIM:[http://omim.org/entry/308100 308100]]. Ichthyosis X-linked is a keratinization disorder manifesting with mild erythroderma and generalized exfoliation of the skin within a few weeks after birth. Affected boys later develop large, polygonal, dark brown scales, especially on the neck, extremities, trunk, and buttocks.<ref>PMID:1539590</ref> <ref>PMID:9252398</ref> <ref>PMID:10679952</ref> <ref>PMID:10844566</ref> | + | [https://www.uniprot.org/uniprot/STS_HUMAN STS_HUMAN] Defects in STS are the cause of ichthyosis X-linked (IXL) [MIM:[https://omim.org/entry/308100 308100]. Ichthyosis X-linked is a keratinization disorder manifesting with mild erythroderma and generalized exfoliation of the skin within a few weeks after birth. Affected boys later develop large, polygonal, dark brown scales, especially on the neck, extremities, trunk, and buttocks.<ref>PMID:1539590</ref> <ref>PMID:9252398</ref> <ref>PMID:10679952</ref> <ref>PMID:10844566</ref> |
| == Function == | | == Function == |
- | [[http://www.uniprot.org/uniprot/STS_HUMAN STS_HUMAN]] Conversion of sulfated steroid precursors to estrogens during pregnancy. | + | [https://www.uniprot.org/uniprot/STS_HUMAN STS_HUMAN] Conversion of sulfated steroid precursors to estrogens during pregnancy. |
| == Evolutionary Conservation == | | == Evolutionary Conservation == |
| [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| <jmolCheckbox> | | <jmolCheckbox> |
| <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/p4/1p49_consurf.spt"</scriptWhenChecked> | | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/p4/1p49_consurf.spt"</scriptWhenChecked> |
- | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> |
| <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
| </jmolCheckbox> | | </jmolCheckbox> |
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| | | |
| ==See Also== | | ==See Also== |
- | *[[Sulfatase|Sulfatase]] | + | *[[Sulfatase 3D structures|Sulfatase 3D structures]] |
| == References == | | == References == |
| <references/> | | <references/> |
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| [[Category: Homo sapiens]] | | [[Category: Homo sapiens]] |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
- | [[Category: Steryl-sulfatase]]
| + | [[Category: Ghosh D]] |
- | [[Category: Ghosh, D]] | + | [[Category: Hernandez-Guzman FG]] |
- | [[Category: Hernandez-Guzman, F G]] | + | [[Category: Higashiyama T]] |
- | [[Category: Higashiyama, T]] | + | [[Category: Osawa Y]] |
- | [[Category: Osawa, Y]] | + | [[Category: Pangborn W]] |
- | [[Category: Pangborn, W]] | + | |
- | [[Category: Dehydroepiandrosterone sulfate]]
| + | |
- | [[Category: Endoplasmic reticulum membrane-bound]]
| + | |
- | [[Category: Estrone sulfate]]
| + | |
- | [[Category: Human placental enzyme]]
| + | |
- | [[Category: Hydrolase]]
| + | |
- | [[Category: Steroid biosynthesis]]
| + | |
- | [[Category: Steroid sulfatase]]
| + | |
| Structural highlights
1p49 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 2.6Å |
Ligands: | , , , , |
Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Disease
STS_HUMAN Defects in STS are the cause of ichthyosis X-linked (IXL) [MIM:308100. Ichthyosis X-linked is a keratinization disorder manifesting with mild erythroderma and generalized exfoliation of the skin within a few weeks after birth. Affected boys later develop large, polygonal, dark brown scales, especially on the neck, extremities, trunk, and buttocks.[1] [2] [3] [4]
Function
STS_HUMAN Conversion of sulfated steroid precursors to estrogens during pregnancy.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Estrone sulfatase (ES; 562 amino acids), one of the key enzymes responsible for maintaining high levels of estrogens in breast tumor cells, is associated with the membrane of the endoplasmic reticulum (ER). The structure of ES, purified from the microsomal fraction of human placentas, has been determined at 2.60-A resolution by x-ray crystallography. This structure shows a domain consisting of two antiparallel alpha-helices that protrude from the roughly spherical molecule, thereby giving the molecule a "mushroom-like" shape. These highly hydrophobic helices, each about 40 A long, are capable of traversing the membrane, thus presumably anchoring the functional domain on the membrane surface facing the ER lumen. The location of the transmembrane domain is such that the opening to the active site, buried deep in a cavity of the "gill" of the "mushroom," rests near the membrane surface, thereby suggesting a role of the lipid bilayer in catalysis. This simple architecture could be a prototype utilized by the ER membrane in dictating the form and the function of ER-resident enzymes.
Structure of human estrone sulfatase suggests functional roles of membrane association.,Hernandez-Guzman FG, Higashiyama T, Pangborn W, Osawa Y, Ghosh D J Biol Chem. 2003 Jun 20;278(25):22989-97. Epub 2003 Mar 25. PMID:12657638[5]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Basler E, Grompe M, Parenti G, Yates J, Ballabio A. Identification of point mutations in the steroid sulfatase gene of three patients with X-linked ichthyosis. Am J Hum Genet. 1992 Mar;50(3):483-91. PMID:1539590
- ↑ Alperin ES, Shapiro LJ. Characterization of point mutations in patients with X-linked ichthyosis. Effects on the structure and function of the steroid sulfatase protein. J Biol Chem. 1997 Aug 15;272(33):20756-63. PMID:9252398
- ↑ Sugawara T, Shimizu H, Hoshi N, Fujimoto Y, Nakajima A, Fujimoto S. PCR diagnosis of X-linked ichthyosis: identification of a novel mutation (E560P) of the steroid sulfatase gene. Hum Mutat. 2000 Mar;15(3):296. PMID:10679952 doi:<296::AID-HUMU17>3.0.CO;2-# 10.1002/(SICI)1098-1004(200003)15:3<296::AID-HUMU17>3.0.CO;2-#
- ↑ Oyama N, Satoh M, Iwatsuki K, Kaneko F. Novel point mutations in the steroid sulfatase gene in patients with X-linked ichthyosis: transfection analysis using the mutated genes. J Invest Dermatol. 2000 Jun;114(6):1195-9. PMID:10844566 doi:jid004
- ↑ Hernandez-Guzman FG, Higashiyama T, Pangborn W, Osawa Y, Ghosh D. Structure of human estrone sulfatase suggests functional roles of membrane association. J Biol Chem. 2003 Jun 20;278(25):22989-97. Epub 2003 Mar 25. PMID:12657638 doi:10.1074/jbc.M211497200
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