4gra - Revision history

OCA at 15:54, 14 March 2024

OCA — Thu, 14 Mar 2024 15:54:08 GMT

←Older revision		Revision as of 15:54, 14 March 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4gra]] 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=4GRA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4GRA FirstGlance]. <br>		<table><tr><td colspan='2'>[[4gra]] 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=4GRA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4GRA 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]] 2.56Å</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=4gra FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gra OCA], [https://pdbe.org/4gra PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4gra RCSB], [https://www.ebi.ac.uk/pdbsum/4gra PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4gra 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=4gra FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gra OCA], [https://pdbe.org/4gra PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4gra RCSB], [https://www.ebi.ac.uk/pdbsum/4gra PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4gra 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>		[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;">
-	== Publication Abstract from PubMed ==
-	Human cytosolic sulfotransferases (SULTs) transfer the sulfuryl moiety (-SO(3)) from activated sulfate [3'-phosphoadenosine 5'-phosphosulfate (PAPS)] to the hydroxyls and primary amines of numerous metabolites, drugs, and xenobiotics. Receipt of the sulfuryl group often radically alters acceptor-target interactions. How these enzymes select particular substrates from the hundreds of candidates in a complex cytosol remains an important question. Recent work reveals PAPS binding causes SULT2A1 to undergo an isomerization that controls selectivity by constricting the opening through which acceptors must pass to enter the active site. The enzyme maintains an affinity for large substrates by isomerizing between the open and closed states with nucleotide bound. Here, the molecular basis of the nucleotide-induced closure is explored in equilibrium and nonequilibrium molecular dynamics simulations. The simulations predict that the active-site "cap," which covers both the nucleotide and acceptor binding sites, opens and closes in response to nucleotide. The cap subdivides into nucleotide and acceptor halves whose motions, while coupled, exhibit an independence that can explain the isomerization. In silico weakening of electrostatic interactions between the cap and base of the active site causes the acceptor half of the cap to open and close while the nucleotide lid remains shut. Simulations predict that SULT1A1, the most abundant SULT in human liver, will utilize a similar selection mechanism. This prediction is tested using fulvestrant, an anti-estrogen too large to pass through the closed pore, and estradiol, which is not restricted by closure. Equilibrium and pre-steady-state binding studies confirm that SULT1A1 undergoes a nucleotide-induced isomerzation that controls substrate selection.
-
-	The gate that governs sulfotransferase selectivity.,Cook I, Wang T, Almo SC, Kim J, Falany CN, Leyh TS Biochemistry. 2013 Jan 15;52(2):415-24. doi: 10.1021/bi301492j. Epub 2012 Dec 28. PMID:23256751<ref>PMID:23256751</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 4gra" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==

OCA at 07:12, 26 October 2022

OCA — Wed, 26 Oct 2022 07:12:27 GMT

←Older revision		Revision as of 07:12, 26 October 2022
Line 1:		Line 1:

	==Crystal structure of SULT1A1 bound with PAP==		==Crystal structure of SULT1A1 bound with PAP==
-	<StructureSection load='4gra' size='340' side='right' caption='[[4gra]], [[Resolution\|resolution]] 2.56Å' scene=''>	+	<StructureSection load='4gra' size='340' side='right'caption='[[4gra]], [[Resolution\|resolution]] 2.56Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4gra]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GRA OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4GRA FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4gra]] 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=4GRA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4GRA FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><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=A3P:ADENOSINE-3-5-DIPHOSPHATE'>A3P</scene></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">SULT1A1, STP, STP1, OK/SW-cl.88 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=4gra FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gra OCA], [https://pdbe.org/4gra PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4gra RCSB], [https://www.ebi.ac.uk/pdbsum/4gra PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4gra ProSAT]</span></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Aryl_sulfotransferase Aryl sulfotransferase], with EC number [http://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'>[~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4gra FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gra OCA], [~~http~~://pdbe.org/4gra PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4gra RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4gra PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4gra ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://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>	+	[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 ==
Line 22:		Line 20:

	==See Also==		==See Also==
-	*[[Sulfotransferase\|Sulfotransferase]]	+	*[[Sulfotransferase 3D structures\|Sulfotransferase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Aryl sulfotransferase~~]]	+	[[Category: Homo sapiens]]
-	[[Category: ~~Human~~]]	+	[[Category: Large Structures]]
-	[[Category: Almo~~, S C~~]]	+	[[Category: Almo SC]]
-	[[Category: Cook, I]]	+	[[Category: Cook I]]
-	[[Category: Falany~~, C N~~]]	+	[[Category: Falany CN]]
-	[[Category: Kim, J]]	+	[[Category: Kim J]]
-	[[Category: Leyh~~, T S~~]]	+	[[Category: Leyh TS]]
-	[[Category: Wang, T]]	+	[[Category: Wang T]]
-	~~[[Category: Estradiol]]~~	+
-	~~[[Category: Hormone regulation]]~~	+
-	~~[[Category: Sulfotransferase]]~~	+
-	~~[[Category: Transferase~~]]	+

OCA at 15:53, 5 August 2016

OCA — Fri, 05 Aug 2016 15:53:44 GMT

←Older revision		Revision as of 15:53, 5 August 2016
Line 1:		Line 1:
		+
	==Crystal structure of SULT1A1 bound with PAP==		==Crystal structure of SULT1A1 bound with PAP==
	<StructureSection load='4gra' size='340' side='right' caption='[[4gra]], [[Resolution\|resolution]] 2.56Å' scene=''>		<StructureSection load='4gra' size='340' side='right' caption='[[4gra]], [[Resolution\|resolution]] 2.56Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4gra]] is a 2 chain structure with 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=4GRA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4GRA FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4gra]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GRA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4GRA FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><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"><scene name='pdbligand=A3P:ADENOSINE-3-5-DIPHOSPHATE'>A3P</scene></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">SULT1A1, STP, STP1, OK/SW-cl.88 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 ~~Homo sapiens~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">SULT1A1, STP, STP1, OK/SW-cl.88 ([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/Aryl_sulfotransferase Aryl sulfotransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.8.2.1 2.8.2.1] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Aryl_sulfotransferase Aryl sulfotransferase], with EC number [http://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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4gra FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gra OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4gra RCSB], [http://www.ebi.ac.uk/pdbsum/4gra 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=4gra FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gra OCA], [http://pdbe.org/4gra PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4gra RCSB], [http://www.ebi.ac.uk/pdbsum/4gra PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4gra ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 18:		Line 19:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 4gra" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 26:		Line 28:
	</StructureSection>		</StructureSection>
	[[Category: Aryl sulfotransferase]]		[[Category: Aryl sulfotransferase]]
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Almo, S C]]		[[Category: Almo, S C]]
	[[Category: Cook, I]]		[[Category: Cook, I]]

OCA at 03:46, 25 December 2014

OCA — Thu, 25 Dec 2014 03:46:00 GMT

←Older revision		Revision as of 03:46, 25 December 2014
Line 8:		Line 8:
	<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=4gra FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gra OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4gra RCSB], [http://www.ebi.ac.uk/pdbsum/4gra 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=4gra FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gra OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4gra RCSB], [http://www.ebi.ac.uk/pdbsum/4gra PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://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 ==

OCA at 09:25, 10 December 2014

OCA — Wed, 10 Dec 2014 09:25:24 GMT

←Older revision		Revision as of 09:25, 10 December 2014
Line 1:		Line 1:
-	[[~~Image:~~4gra.~~png~~\|~~left~~\|~~200px~~]]	+	==Crystal structure of SULT1A1 bound with PAP==
		+	<StructureSection load='4gra' size='340' side='right' caption='[[4gra]], [[Resolution\|resolution]] 2.56Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[4gra]] is a 2 chain structure with 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=4GRA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4GRA FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=A3P:ADENOSINE-3-5-DIPHOSPHATE'>A3P</scene></td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">SULT1A1, STP, STP1, OK/SW-cl.88 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Aryl_sulfotransferase Aryl sulfotransferase], with EC number [http://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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4gra FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gra OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4gra RCSB], [http://www.ebi.ac.uk/pdbsum/4gra PDBsum]</span></td></tr>
		+	</table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Human cytosolic sulfotransferases (SULTs) transfer the sulfuryl moiety (-SO(3)) from activated sulfate [3'-phosphoadenosine 5'-phosphosulfate (PAPS)] to the hydroxyls and primary amines of numerous metabolites, drugs, and xenobiotics. Receipt of the sulfuryl group often radically alters acceptor-target interactions. How these enzymes select particular substrates from the hundreds of candidates in a complex cytosol remains an important question. Recent work reveals PAPS binding causes SULT2A1 to undergo an isomerization that controls selectivity by constricting the opening through which acceptors must pass to enter the active site. The enzyme maintains an affinity for large substrates by isomerizing between the open and closed states with nucleotide bound. Here, the molecular basis of the nucleotide-induced closure is explored in equilibrium and nonequilibrium molecular dynamics simulations. The simulations predict that the active-site "cap," which covers both the nucleotide and acceptor binding sites, opens and closes in response to nucleotide. The cap subdivides into nucleotide and acceptor halves whose motions, while coupled, exhibit an independence that can explain the isomerization. In silico weakening of electrostatic interactions between the cap and base of the active site causes the acceptor half of the cap to open and close while the nucleotide lid remains shut. Simulations predict that SULT1A1, the most abundant SULT in human liver, will utilize a similar selection mechanism. This prediction is tested using fulvestrant, an anti-estrogen too large to pass through the closed pore, and estradiol, which is not restricted by closure. Equilibrium and pre-steady-state binding studies confirm that SULT1A1 undergoes a nucleotide-induced isomerzation that controls substrate selection.

-	~~{{STRUCTURE_4gra\| PDB=4gra \| SCENE= }}~~	+	The gate that governs sulfotransferase selectivity.,Cook I, Wang T, Almo SC, Kim J, Falany CN, Leyh TS Biochemistry. 2013 Jan 15;52(2):415-24. doi: 10.1021/bi301492j. Epub 2012 Dec 28. PMID:23256751<ref>PMID:23256751</ref>

-	~~===Crystal structure~~ of ~~SULT1A1 bound with PAP===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>

-	~~{{ABSTRACT_PUBMED_23256751}}~~	+	==See Also==
-		+	*[[Sulfotransferase\|Sulfotransferase]]
-	==~~About this Structure~~==	+	== References ==
-	[[~~4gra~~]] ~~is a 2 chain structure with 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=4GRA OCA].~~	+	<references/>
		+	__TOC__
		+	</StructureSection>
	[[Category: Aryl sulfotransferase]]		[[Category: Aryl sulfotransferase]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
-	[[Category: Almo, S C.]]	+	[[Category: Almo, S C]]
-	[[Category: Cook, I.]]	+	[[Category: Cook, I]]
-	[[Category: Falany, C N.]]	+	[[Category: Falany, C N]]
-	[[Category: Kim, J.]]	+	[[Category: Kim, J]]
-	[[Category: Leyh, T S.]]	+	[[Category: Leyh, T S]]
-	[[Category: Wang, T.]]	+	[[Category: Wang, T]]
	[[Category: Estradiol]]		[[Category: Estradiol]]
	[[Category: Hormone regulation]]		[[Category: Hormone regulation]]
	[[Category: Sulfotransferase]]		[[Category: Sulfotransferase]]
	[[Category: Transferase]]		[[Category: Transferase]]

OCA at 12:07, 23 January 2013

OCA — Wed, 23 Jan 2013 12:07:03 GMT

←Older revision		Revision as of 12:07, 23 January 2013
Line 1:		Line 1:
-	[[Image:4gra.~~jpg~~\|left\|200px]]	+	[[Image:4gra.png\|left\|200px]]

	{{STRUCTURE_4gra\| PDB=4gra \| SCENE= }}		{{STRUCTURE_4gra\| PDB=4gra \| SCENE= }}

OCA at 08:51, 16 January 2013

OCA — Wed, 16 Jan 2013 08:51:03 GMT

←Older revision		Revision as of 08:51, 16 January 2013
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	[[Image:4gra.jpg\|left\|200px]]

-	~~The entry~~ 4gra ~~is ON HOLD~~	+	{{STRUCTURE_4gra\| PDB=4gra \| SCENE= }}

-	~~Authors: Kim, J., Cook, I., Wang, T., Falany, C.N., Leyh, T.S., Almo, S.C.~~	+	===Crystal structure of SULT1A1 bound with PAP===

-	~~Description: Crystal~~ structure ~~of SULT1A1 bound~~ with ~~PAP~~	+	{{ABSTRACT_PUBMED_23256751}}
		+
		+	==About this Structure==
		+	[[4gra]] is a 2 chain structure with 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=4GRA OCA].
		+	[[Category: Aryl sulfotransferase]]
		+	[[Category: Homo sapiens]]
		+	[[Category: Almo, S C.]]
		+	[[Category: Cook, I.]]
		+	[[Category: Falany, C N.]]
		+	[[Category: Kim, J.]]
		+	[[Category: Leyh, T S.]]
		+	[[Category: Wang, T.]]
		+	[[Category: Estradiol]]
		+	[[Category: Hormone regulation]]
		+	[[Category: Sulfotransferase]]
		+	[[Category: Transferase]]

OCA: Protected "4gra" [edit=sysop:move=sysop]

OCA — Wed, 05 Sep 2012 04:56:42 GMT

Protected "4gra" [edit=sysop:move=sysop]

←Older revision

Revision as of 04:56, 5 September 2012

OCA: New page: '''Unreleased structure''' The entry 4gra is ON HOLD Authors: Kim, J., Cook, I., Wang, T., Falany, C.N., Leyh, T.S., Almo, S.C. Description: Crystal structure of SULT1A1 bound with PAP

OCA — Wed, 05 Sep 2012 04:56:41 GMT

New page: '''Unreleased structure''' The entry 4gra is ON HOLD Authors: Kim, J., Cook, I., Wang, T., Falany, C.N., Leyh, T.S., Almo, S.C. Description: Crystal structure of SULT1A1 bound with PAP

New page

'''Unreleased structure'''

The entry 4gra is ON HOLD

Authors: Kim, J., Cook, I., Wang, T., Falany, C.N., Leyh, T.S., Almo, S.C.

Description: Crystal structure of SULT1A1 bound with PAP