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[[Image:1hy3.gif|left|200px]]


{{Structure
==CRYSTAL STRUCTURE OF HUMAN ESTROGEN SULFOTRANSFERASE V269E MUTANT IN THE PRESENCE OF PAPS==
|PDB= 1hy3 |SIZE=350|CAPTION= <scene name='initialview01'>1hy3</scene>, resolution 1.80&Aring;
<StructureSection load='1hy3' size='340' side='right'caption='[[1hy3]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=PPS:3'-PHOSPHATE-ADENOSINE-5'-PHOSPHATE SULFATE'>PPS</scene>
<table><tr><td colspan='2'>[[1hy3]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HY3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HY3 FirstGlance]. <br>
|ACTIVITY= [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]  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
|GENE= STE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PPS:3-PHOSPHATE-ADENOSINE-5-PHOSPHATE+SULFATE'>PPS</scene></td></tr>
}}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1hy3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hy3 OCA], [https://pdbe.org/1hy3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hy3 RCSB], [https://www.ebi.ac.uk/pdbsum/1hy3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hy3 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ST1E1_HUMAN 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.<ref>PMID:11884392</ref>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hy/1hy3_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1hy3 ConSurf].
<div style="clear:both"></div>


'''CRYSTAL STRUCTURE OF HUMAN ESTROGEN SULFOTRANSFERASE V269E MUTANT IN THE PRESENCE OF PAPS'''
==See Also==
 
*[[Sulfotransferase|Sulfotransferase]]
 
*[[Sulfotransferase 3D structures|Sulfotransferase 3D structures]]
==Overview==
== References ==
Estrogen sulfotransferase (EST) transfers the sulfate group from 3'-phosphoadenosine 5'-phosphosulfate (PAPS) to estrogenic steroids. Here we report the crystal structure of human EST (hEST) in the context of the V269E mutant-PAPS complex, which is the first structure containing the active sulfate donor for any sulfotransferase. Superimposing this structure with the crystal structure of hEST in complex with the donor product 3'-phosphoadenosine 5'-phosphate (PAP) and the acceptor substrate 17beta-estradiol, the ternary structure with the PAPS and estradiol molecule, is modeled. These structures have now provided a more complete view of the S(N)2-like in-line displacement reaction catalyzed by sulfotransferases. In the PAPS-bound structure, the side chain nitrogen of the catalytic Lys(47) interacts with the side chain hydroxyl of Ser(137) and not with the bridging oxygen between the 5'-phosphate and sulfate groups of the PAPS molecule as is seen in the PAP-bound structures. This conformational change of the side chain nitrogen indicates that the interaction of Lys(47) with Ser(137) may regulate PAPS hydrolysis in the absences of an acceptor substrate. Supporting the structural data, the mutations of Ser(137) to cysteine and alanine decrease gradually k(cat) for PAPS hydrolysis and transfer activity. Thus, Ser(137) appears to play an important role in regulating the side chain interaction of Lys(47) with the bridging oxygen between the 5'-phosphate and the sulfate of PAPS.
<references/>
 
__TOC__
==Disease==
</StructureSection>
Known diseases associated with this structure: Mandibuloacral dysplasia with type B lipodystrophy OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=606480 606480]], Restrictive dermopathy, lethal OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=606480 606480]]
 
==About this Structure==
1HY3 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HY3 OCA].
 
==Reference==
Crystal structure of the human estrogen sulfotransferase-PAPS complex: evidence for catalytic role of Ser137 in the sulfuryl transfer reaction., Pedersen LC, Petrotchenko E, Shevtsov S, Negishi M, J Biol Chem. 2002 May 17;277(20):17928-32. Epub 2002 Mar 7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11884392 11884392]
[[Category: Estrone sulfotransferase]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Negishi, M.]]
[[Category: Negishi M]]
[[Category: Pedersen, L C.]]
[[Category: Pedersen LC]]
[[Category: Petrochenko, E V.]]
[[Category: Petrochenko EV]]
[[Category: Shevtsov, S.]]
[[Category: Shevtsov S]]
[[Category: PPS]]
[[Category: estrogen]]
[[Category: human]]
[[Category: pap]]
[[Category: sulfotransferase]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:43:00 2008''

Latest revision as of 10:31, 7 February 2024

CRYSTAL STRUCTURE OF HUMAN ESTROGEN SULFOTRANSFERASE V269E MUTANT IN THE PRESENCE OF PAPSCRYSTAL STRUCTURE OF HUMAN ESTROGEN SULFOTRANSFERASE V269E MUTANT IN THE PRESENCE OF PAPS

Structural highlights

1hy3 is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.8Å
Ligands:
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.

See Also

References

  1. ↑ 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

1hy3, resolution 1.80Å

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