1p49

From Proteopedia

(Difference between revisions)

Revision as of 03:38, 11 September 2015

Structure of Human Placental Estrone/DHEA 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.
Ligands:	, , ,
NonStd Res:
Activity:	Steryl-sulfatase, with EC number 3.1.6.2
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

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.

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

1 Structural highlights
2 Disease
3 Function
4 Evolutionary Conservation
5 Publication Abstract from PubMed
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1p49"

@@ Line 6: / Line 6: @@
 <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ALS:2-AMINO-3-OXO-4-SULFO-BUTYRIC+ACID'>ALS</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'>[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://www.rcsb.org/pdb/explore.do?structureId=1p49 RCSB], [http://www.ebi.ac.uk/pdbsum/1p49 PDBsum]</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]</span></td></tr>
 </table>
 == Disease ==
@@ Line 30: / Line 30: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 1p49" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

1p49

From Proteopedia

Revision as of 03:38, 11 September 2015

Structure of Human Placental Estrone/DHEA Sulfatase

Structural highlights

Disease

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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