1bo6: Difference between revisions
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==ESTROGEN SULFOTRANSFERASE WITH INACTIVE COFACTOR PAP AND VANADATE== | ==ESTROGEN SULFOTRANSFERASE WITH INACTIVE COFACTOR PAP AND VANADATE== | ||
<StructureSection load='1bo6' size='340' side='right' caption='[[1bo6]], [[Resolution|resolution]] 2.10Å' scene=''> | <StructureSection load='1bo6' size='340' side='right' caption='[[1bo6]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1bo6]] is a 2 chain structure | <table><tr><td colspan='2'>[[1bo6]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BO6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BO6 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>, <scene name='pdbligand=VO4:VANADATE+ION'>VO4</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>, <scene name='pdbligand=VO4:VANADATE+ION'>VO4</scene></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='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=1bo6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bo6 OCA], [http://pdbe.org/1bo6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1bo6 RCSB], [http://www.ebi.ac.uk/pdbsum/1bo6 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=1bo6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bo6 OCA], [http://pdbe.org/1bo6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1bo6 RCSB], [http://www.ebi.ac.uk/pdbsum/1bo6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1bo6 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </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/ | </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=1bo6 ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Estrone sulfotransferase]] | [[Category: Estrone sulfotransferase]] | ||
[[Category: Kakuta, Y]] | [[Category: Kakuta, Y]] | ||
[[Category: Negishi, M]] | [[Category: Negishi, M]] | ||
Revision as of 09:17, 17 August 2017
ESTROGEN SULFOTRANSFERASE WITH INACTIVE COFACTOR PAP AND VANADATEESTROGEN SULFOTRANSFERASE WITH INACTIVE COFACTOR PAP AND VANADATE
Structural highlights
Function[ST1E1_MOUSE] 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. 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 PubMedEstrogen sulfotransferase (EST) catalyzes transfer of the 5'-sulfuryl group of adenosine 3'-phosphate 5'-phosphosulfate (PAPS) to the 3alpha-phenol group of estrogenic steroids such as estradiol (E2). The recent crystal structure of EST-adenosine 3', 5'-diphosphate (PAP)- E2 complex has revealed that residues Lys48, Thr45, Thr51, Thr52, Lys106, His108, and Try240 are in position to play a catalytic role in the sulfuryl transfer reaction of EST (Kakuta Y., Pedersen, L. G., Carter, C. W., Negishi, M., and Pedersen, L. C. (1997) Nat. Struct. Biol. 4, 904-908). Mutation of Lys48, Lys106, or His108 nearly abolishes EST activity, indicating that they play a critical role in catalysis. A present 2.2-A resolution structure of EST-PAP-vanadate complex indicates that the vanadate molecule adopts a trigonal bipyramidal geometry with its equatorial oxygens coordinated to these three residues. The apical positions of the vanadate molecule are occupied by a terminal oxygen of the 5'-phosphate of PAP (2.1 A) and a possible water molecule (2. 3 A). This water molecule superimposes well to the 3alpha-phenol group of E2 in the crystal structure of the EST.PAP.E2 complex. These structures are characteristic of the transition state for an in-line sulfuryl transfer reaction from PAPS to E2. Moreover, residues Lys48, Lys106, and His108 are found to be coordinated with the vanadate molecule at the transition state of EST. The sulfuryl transfer mechanism. Crystal structure of a vanadate complex of estrogen sulfotransferase and mutational analysis.,Kakuta Y, Petrotchenko EV, Pedersen LC, Negishi M J Biol Chem. 1998 Oct 16;273(42):27325-30. PMID:9765259[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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