1g3m

CRYSTAL STRUCTURE OF HUMAN ESTROGEN SULFOTRANSFERASE IN COMPLEX WITH IN-ACTIVE COFACTOR PAP AND 3,5,3',5'-TETRACHLORO-BIPHENYL-4,4'-DIOLCRYSTAL STRUCTURE OF HUMAN ESTROGEN SULFOTRANSFERASE IN COMPLEX WITH IN-ACTIVE COFACTOR PAP AND 3,5,3',5'-TETRACHLORO-BIPHENYL-4,4'-DIOL

Structural highlights 1g3m is a 2 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: , , Gene: STE (HUMAN) Activity: Estrone sulfotransferase, with EC number 2.8.2.4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [ST1E1_HUMAN] Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of estradiol and estrone. May play a role in the regulation of estrogen receptor activity by metabolizing free estradiol. Maximally sulfates beta-estradiol and estrone at concentrations of 20 nM. Also sulfates dehydroepiandrosterone, pregnenolone, ethinylestradiol, equalenin, diethylstilbesterol and 1-naphthol, at significantly higher concentrations; however, cortisol, testosterone and dopamine are not sulfated. 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 Certain hydroxylated polychlorinated biphenyls (OH-PCBs) inhibit the human estrogen sulfotransferase (hEST) at subnanomolar concentrations, suggesting a possible pathway for PCB toxicity due to environmental exposure in humans. To address the structural basis of the inhibition, we have determined the crystal structure of hEST in the presence of the sulfuryl donor product 3 -phosphoadenosine 5 -phosphate and the OH-PCB 4,4 -OH 3,5,3,5 -tetraCB. The OH-PCB binds in the estrogen binding site with the position of the first phenolic ring in an orientation similar to the phenolic ring of 17 beta-estradiol. Interestingly, the OH-PCB does not bind in a planar conformation, but rather with a 30-degree twist between the phenyl rings. The crystal structure of hEST with the OH-PCB bound gives physical evidence that certain OH-PCBs can mimic binding of estrogenic compounds in biological systems. Crystallographic analysis of a hydroxylated polychlorinated biphenyl (OH-PCB) bound to the catalytic estrogen binding site of human estrogen sulfotransferase.,Shevtsov S, Petrotchenko EV, Pedersen LC, Negishi M Environ Health Perspect. 2003 Jun;111(7):884-8. PMID:12782487 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

spinqualitylabelsall models 1g3m, resolution 1.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image