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| | <StructureSection load='2h8k' size='340' side='right'caption='[[2h8k]], [[Resolution|resolution]] 3.20Å' scene=''> | | <StructureSection load='2h8k' size='340' side='right'caption='[[2h8k]], [[Resolution|resolution]] 3.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2h8k]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H8K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2H8K FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2h8k]] 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=2H8K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2H8K FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=A3P:ADENOSINE-3-5-DIPHOSPHATE'>A3P</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.2Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SULT1C3 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=A3P:ADENOSINE-3-5-DIPHOSPHATE'>A3P</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=2h8k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h8k OCA], [https://pdbe.org/2h8k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2h8k RCSB], [https://www.ebi.ac.uk/pdbsum/2h8k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2h8k ProSAT]</span></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=2h8k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h8k OCA], [https://pdbe.org/2h8k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2h8k RCSB], [https://www.ebi.ac.uk/pdbsum/2h8k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2h8k ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/ST1C3_HUMAN ST1C3_HUMAN]] Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor and has low sulphotransferase activity towards various substrates with alcohol groups (in vitro). May catalyze the sulfate conjugation of xenobiotic compounds and endogenous substrates.<ref>PMID:17936463</ref> <ref>PMID:17425406</ref>
| + | [https://www.uniprot.org/uniprot/ST1C3_HUMAN ST1C3_HUMAN] Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor and has low sulphotransferase activity towards various substrates with alcohol groups (in vitro). May catalyze the sulfate conjugation of xenobiotic compounds and endogenous substrates.<ref>PMID:17936463</ref> <ref>PMID:17425406</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | | | |
| | ==See Also== | | ==See Also== |
| - | *[[Sulfotransferase|Sulfotransferase]] | + | *[[Sulfotransferase 3D structures|Sulfotransferase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Arrowsmith, C H]] | + | [[Category: Arrowsmith CH]] |
| - | [[Category: Bochkarev, A]] | + | [[Category: Bochkarev A]] |
| - | [[Category: Dombrovski, L]] | + | [[Category: Dombrovski L]] |
| - | [[Category: Edwards, A M]] | + | [[Category: Edwards AM]] |
| - | [[Category: Loppnau, P]] | + | [[Category: Loppnau P]] |
| - | [[Category: Plotnikov, A N]] | + | [[Category: Plotnikov AN]] |
| - | [[Category: Structural genomic]]
| + | [[Category: Sundstrom M]] |
| - | [[Category: Sundstrom, M]] | + | [[Category: Tempel W]] |
| - | [[Category: Tempel, W]] | + | [[Category: Weigelt J]] |
| - | [[Category: Weigelt, J]] | + | |
| - | [[Category: Pap]]
| + | |
| - | [[Category: Sgc]]
| + | |
| - | [[Category: Sulfate conjugation]]
| + | |
| - | [[Category: Sulfotransferase]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
ST1C3_HUMAN Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor and has low sulphotransferase activity towards various substrates with alcohol groups (in vitro). May catalyze the sulfate conjugation of xenobiotic compounds and endogenous substrates.[1] [2]
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
The human cytosolic sulfotransfases (hSULTs) comprise a family of 12 phase II enzymes involved in the metabolism of drugs and hormones, the bioactivation of carcinogens, and the detoxification of xenobiotics. Knowledge of the structural and mechanistic basis of substrate specificity and activity is crucial for understanding steroid and hormone metabolism, drug sensitivity, pharmacogenomics, and response to environmental toxins. We have determined the crystal structures of five hSULTs for which structural information was lacking, and screened nine of the 12 hSULTs for binding and activity toward a panel of potential substrates and inhibitors, revealing unique "chemical fingerprints" for each protein. The family-wide analysis of the screening and structural data provides a comprehensive, high-level view of the determinants of substrate binding, the mechanisms of inhibition by substrates and environmental toxins, and the functions of the orphan family members SULT1C3 and SULT4A1. Evidence is provided for structural "priming" of the enzyme active site by cofactor binding, which influences the spectrum of small molecules that can bind to each enzyme. The data help explain substrate promiscuity in this family and, at the same time, reveal new similarities between hSULT family members that were previously unrecognized by sequence or structure comparison alone.
Structural and chemical profiling of the human cytosolic sulfotransferases.,Allali-Hassani A, Pan PW, Dombrovski L, Najmanovich R, Tempel W, Dong A, Loppnau P, Martin F, Thornton J, Edwards AM, Bochkarev A, Plotnikov AN, Vedadi M, Arrowsmith CH PLoS Biol. 2007 May;5(5):e97. PMID:17425406[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Meinl W, Donath C, Schneider H, Sommer Y, Glatt H. SULT1C3, an orphan sequence of the human genome, encodes an enzyme activating various promutagens. Food Chem Toxicol. 2008 Apr;46(4):1249-56. Epub 2007 Sep 6. PMID:17936463 doi:http://dx.doi.org/10.1016/j.fct.2007.08.040
- ↑ Allali-Hassani A, Pan PW, Dombrovski L, Najmanovich R, Tempel W, Dong A, Loppnau P, Martin F, Thornton J, Edwards AM, Bochkarev A, Plotnikov AN, Vedadi M, Arrowsmith CH. Structural and chemical profiling of the human cytosolic sulfotransferases. PLoS Biol. 2007 May;5(5):e97. PMID:17425406 doi:10.1371/journal.pbio.0050097
- ↑ Allali-Hassani A, Pan PW, Dombrovski L, Najmanovich R, Tempel W, Dong A, Loppnau P, Martin F, Thornton J, Edwards AM, Bochkarev A, Plotnikov AN, Vedadi M, Arrowsmith CH. Structural and chemical profiling of the human cytosolic sulfotransferases. PLoS Biol. 2007 May;5(5):e97. PMID:17425406 doi:10.1371/journal.pbio.0050097
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