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==Crystal structure of hSULT1A1 bound to PAP and 2-Naphtol== | ==Crystal structure of hSULT1A1 bound to PAP and 2-Naphtol== | ||
<StructureSection load='3u3k' size='340' side='right' caption='[[3u3k]], [[Resolution|resolution]] 2.36Å' scene=''> | <StructureSection load='3u3k' size='340' side='right'caption='[[3u3k]], [[Resolution|resolution]] 2.36Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3u3k]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3u3k]] 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=3U3K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3U3K FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=03V:NAPHTHALEN-2-OL'>03V</scene>, <scene name='pdbligand=A3P:ADENOSINE-3-5-DIPHOSPHATE'>A3P</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=03V:NAPHTHALEN-2-OL'>03V</scene>, <scene name='pdbligand=A3P:ADENOSINE-3-5-DIPHOSPHATE'>A3P</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3u3j|3u3j]], [[3u3m|3u3m]], [[3u3o|3u3o]], [[3u3r|3u3r]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3u3j|3u3j]], [[3u3m|3u3m]], [[3u3o|3u3o]], [[3u3r|3u3r]]</div></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">hSULT1A1, OK/SW-cl.88, STP, STP1, SULT1A1 ([ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">hSULT1A1, OK/SW-cl.88, STP, STP1, SULT1A1 ([https://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'>[ | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Aryl_sulfotransferase Aryl sulfotransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.8.2.1 2.8.2.1] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3u3k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3u3k OCA], [https://pdbe.org/3u3k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3u3k RCSB], [https://www.ebi.ac.uk/pdbsum/3u3k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3u3k ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/ST1A1_HUMAN ST1A1_HUMAN]] Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of catecholamines, phenolic drugs and neurotransmitters. Has also estrogen sulfotransferase activity. responsible for the sulfonation and activation of minoxidil. Is Mediates the metabolic activation of carcinogenic N-hydroxyarylamines to DNA binding products and could so participate as modulating factor of cancer risk.<ref>PMID:12471039</ref> <ref>PMID:16221673</ref> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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==See Also== | ==See Also== | ||
*[[Sulfotransferase|Sulfotransferase]] | *[[Sulfotransferase 3D structures|Sulfotransferase 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
| Line 30: | Line 30: | ||
[[Category: Aryl sulfotransferase]] | [[Category: Aryl sulfotransferase]] | ||
[[Category: Human]] | [[Category: Human]] | ||
[[Category: Large Structures]] | |||
[[Category: Aharoni, A]] | [[Category: Aharoni, A]] | ||
[[Category: Berger, I]] | [[Category: Berger, I]] | ||
Revision as of 08:56, 13 July 2022
Crystal structure of hSULT1A1 bound to PAP and 2-NaphtolCrystal structure of hSULT1A1 bound to PAP and 2-Naphtol
Structural highlights
Function[ST1A1_HUMAN] Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of catecholamines, phenolic drugs and neurotransmitters. Has also estrogen sulfotransferase activity. responsible for the sulfonation and activation of minoxidil. Is Mediates the metabolic activation of carcinogenic N-hydroxyarylamines to DNA binding products and could so participate as modulating factor of cancer risk.[1] [2] Publication Abstract from PubMedCytosolic sulfotransferases (SULTs) are mammalian enzymes that detoxify a wide variety of chemicals through the addition of a sulfate group. Despite extensive research, the molecular basis for the broad specificity of SULTs is still not understood. Here, structural, protein engineering and kinetic approaches were employed to obtain deep understanding of the molecular basis for the broad specificity, catalytic activity and substrate inhibition of SULT1A1. We have determined five new structures of SULT1A1 in complex with different acceptors, and utilized a directed evolution approach to generate SULT1A1 mutants with enhanced thermostability and increased catalytic activity. We found that active site plasticity enables binding of different acceptors and identified dramatic structural changes in the SULT1A1 active site leading to the binding of a second acceptor molecule in a conserved yet non-productive manner. Our combined approach highlights the dominant role of SULT1A1 structural flexibility in controlling the specificity and activity of this enzyme. The molecular basis for the broad substrate specificity of human sulfotransferase 1A1.,Berger I, Guttman C, Amar D, Zarivach R, Aharoni A PLoS One. 2011;6(11):e26794. Epub 2011 Nov 1. PMID:22069470[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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