1p49: Difference between revisions
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|PDB= 1p49 |SIZE=350|CAPTION= <scene name='initialview01'>1p49</scene>, resolution 2.60Å | |PDB= 1p49 |SIZE=350|CAPTION= <scene name='initialview01'>1p49</scene>, resolution 2.60Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=ALS:2-AMINO-3-OXO-4-SULFO-BUTYRIC+ACID'>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> | ||
|ACTIVITY= [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] | |ACTIVITY= <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> | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<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.ebi.ac.uk/pdbsum/1p49 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1p49 RCSB]</span> | |||
}} | }} | ||
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==Overview== | ==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. | 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. | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Osawa, Y.]] | [[Category: Osawa, Y.]] | ||
[[Category: Pangborn, W.]] | [[Category: Pangborn, W.]] | ||
[[Category: dehydroepiandrosterone sulfate]] | [[Category: dehydroepiandrosterone sulfate]] | ||
[[Category: endoplasmic reticulum membrane-bound]] | [[Category: endoplasmic reticulum membrane-bound]] | ||
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[[Category: steroid sulfatase]] | [[Category: steroid sulfatase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:54:37 2008'' | ||
