1p49 | pdb_00001p49
Structure of Human Placental Estrone/DHEA Sulfatase
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| 1p49, resolution 2.60Å | |||||||||||||
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| Ligands: | BOG, NAG, CA and PO4 | ||||||||||||
| Activity: | Steryl-sulfatase, with EC number 3.1.6.2 | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
Overview
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.
Disease
Known diseases associated with this structure: Ichthyosis, X-linked OMIM:[308100], Placental steroid sulfatase deficiency OMIM:[308100]
About this Structure
1P49 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Mar 20 13:19:39 2008
