1P49

Structure of Human Placental Estrone/DHEA Sulfatase

Summary for 1P49

• Entry DOI: 10.2210/pdb1p49/pdb
• Descriptor: STERYL-SULFATASE, octyl beta-D-glucopyranoside, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (6 entities in total)
• Functional Keywords: steroid biosynthesis, steroid sulfatase, estrone sulfate, dehydroepiandrosterone sulfate, human placental enzyme, endoplasmic reticulum membrane-bound, hydrolase
• Biological source: Homo sapiens (human)
• Cellular location: Endoplasmic reticulum membrane; Multi-pass membrane protein: P08842
• Total number of polymer chains: 1
• Total formula weight: 64214.03

Authors

Hernandez-Guzman, F.G.,Higashiyama, T.,Pangborn, W.,Osawa, Y.,Ghosh, D. (deposition date: 2003-04-21, release date: 2003-08-12, Last modification date: 2020-07-29)

Primary citation

Hernandez-Guzman, F.G.,Higashiyama, T.,Pangborn, W.,Osawa, Y.,Ghosh, D.
Structure of Human Estrone Sulfatase Suggests Functional Roles of Membrane Association
J.Biol.Chem., 278:22989-22997, 2003

PubMed Abstract: 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.

PubMed: 12657638
DOI: 10.1074/jbc.M211497200

Experimental method

X-RAY DIFFRACTION (2.6 Å)