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1g3m

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Revision as of 06:31, 3 January 2018

CRYSTAL 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.^[1]

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^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Pedersen LC, Petrotchenko E, Shevtsov S, Negishi M. Crystal structure of the human estrogen sulfotransferase-PAPS complex: evidence for catalytic role of Ser137 in the sulfuryl transfer reaction. J Biol Chem. 2002 May 17;277(20):17928-32. Epub 2002 Mar 7. PMID:11884392 doi:http://dx.doi.org/10.1074/jbc.M111651200
↑ Shevtsov S, Petrotchenko EV, Pedersen LC, Negishi M. Crystallographic analysis of a hydroxylated polychlorinated biphenyl (OH-PCB) bound to the catalytic estrogen binding site of human estrogen sulfotransferase. Environ Health Perspect. 2003 Jun;111(7):884-8. PMID:12782487

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1g3m"

@@ Line 1: / Line 1: @@
 ==CRYSTAL STRUCTURE OF HUMAN ESTROGEN SULFOTRANSFERASE IN COMPLEX WITH IN-ACTIVE COFACTOR PAP AND 3,5,3',5'-TETRACHLORO-BIPHENYL-4,4'-DIOL==
 <StructureSection load='1g3m' size='340' side='right' caption='[[1g3m]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">STE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Estrone_sulfotransferase Estrone sulfotransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.8.2.4 2.8.2.4] </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=1g3m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g3m OCA], [http://pdbe.org/1g3m PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1g3m RCSB], [http://www.ebi.ac.uk/pdbsum/1g3m 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=1g3m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g3m OCA], [http://pdbe.org/1g3m PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1g3m RCSB], [http://www.ebi.ac.uk/pdbsum/1g3m PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1g3m ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 14: / Line 15: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/g3/1g3m_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/g3/1g3m_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 29: / Line 30: @@
 </div>
 <div class="pdbe-citations 1g3m" style="background-color:#fffaf0;"></div>
-==See Also==
-*[[Sulfotransferase|Sulfotransferase]]
 == References ==
 <references/>

1g3m

From Proteopedia

Revision as of 06:31, 3 January 2018

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

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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