1ov4

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[[Image:1ov4.jpg|left|200px]]
 
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{{Structure
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==Crystal structure of human DHEA-ST complexed with androsterone==
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|PDB= 1ov4 |SIZE=350|CAPTION= <scene name='initialview01'>1ov4</scene>, resolution 2.7&Aring;
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<StructureSection load='1ov4' size='340' side='right'caption='[[1ov4]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=AE2:AETIOCHOLANOLONE'>AE2</scene>
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<table><tr><td colspan='2'>[[1ov4]] is a 1 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=1OV4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OV4 FirstGlance]. <br>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Alcohol_sulfotransferase Alcohol sulfotransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.8.2.2 2.8.2.2]
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7&#8491;</td></tr>
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|GENE= SULT2A1 OR STD OR HST ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AOX:(3BETA,5ALPHA)-3-HYDROXYANDROSTAN-17-ONE'>AOX</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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}}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ov4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ov4 OCA], [https://pdbe.org/1ov4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ov4 RCSB], [https://www.ebi.ac.uk/pdbsum/1ov4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ov4 ProSAT]</span></td></tr>
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</table>
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'''Crystal structure of human DHEA-ST complexed with androsterone'''
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== Function ==
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[https://www.uniprot.org/uniprot/ST2A1_HUMAN ST2A1_HUMAN] Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfonation of steroids and bile acids in the liver and adrenal glands.
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== Evolutionary Conservation ==
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==Overview==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ov/1ov4_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1ov4 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
In steroid biosynthesis, human dehydroepiandrosterone sulfotransferase (DHEA-ST) in the adrenals has been reported to catalyze the transfer of the sulfonate group from 3'-phosphoadenosine-5'-phosphosulfate to dehydroepiandrosterone (DHEA). DHEA and its sulfate play roles as steroid precursors; however, the role of the enzyme in the catabolism of androgens is poorly understood. Androsterone sulfate is clinically recognized as one of the major androgen metabolites found in urine. Here it is demonstrated that this enzyme recognizes androsterone (ADT) as a cognate substrate with similar kinetics but a 2-fold specificity and stronger substrate inhibition than DHEA. The structure of human DHEA-ST in complex with ADT has been solved at 2.7 A resolution, confirming ADT recognition. Structural analysis has revealed the binding mode of ADT differs from that of DHEA, despite the similarity of the overall structure between the ADT and the DHEA binary complexes. Our results identify that this human enzyme is an ADT sulfotransferase as well as a DHEA sulfotransferase, implying an important role in steroid homeostasis for the adrenals and liver.
In steroid biosynthesis, human dehydroepiandrosterone sulfotransferase (DHEA-ST) in the adrenals has been reported to catalyze the transfer of the sulfonate group from 3'-phosphoadenosine-5'-phosphosulfate to dehydroepiandrosterone (DHEA). DHEA and its sulfate play roles as steroid precursors; however, the role of the enzyme in the catabolism of androgens is poorly understood. Androsterone sulfate is clinically recognized as one of the major androgen metabolites found in urine. Here it is demonstrated that this enzyme recognizes androsterone (ADT) as a cognate substrate with similar kinetics but a 2-fold specificity and stronger substrate inhibition than DHEA. The structure of human DHEA-ST in complex with ADT has been solved at 2.7 A resolution, confirming ADT recognition. Structural analysis has revealed the binding mode of ADT differs from that of DHEA, despite the similarity of the overall structure between the ADT and the DHEA binary complexes. Our results identify that this human enzyme is an ADT sulfotransferase as well as a DHEA sulfotransferase, implying an important role in steroid homeostasis for the adrenals and liver.
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==Disease==
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Identifying androsterone (ADT) as a cognate substrate for human dehydroepiandrosterone sulfotransferase (DHEA-ST) important for steroid homeostasis: structure of the enzyme-ADT complex.,Chang HJ, Shi R, Rehse P, Lin SX J Biol Chem. 2004 Jan 23;279(4):2689-96. Epub 2003 Oct 21. PMID:14573603<ref>PMID:14573603</ref>
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Known diseases associated with this structure: Histidinemia OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=609457 609457]], Selective T-cell defect OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=176947 176947]]
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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1OV4 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=1OV4 OCA].
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</div>
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<div class="pdbe-citations 1ov4" style="background-color:#fffaf0;"></div>
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==Reference==
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==See Also==
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Identifying androsterone (ADT) as a cognate substrate for human dehydroepiandrosterone sulfotransferase (DHEA-ST) important for steroid homeostasis: structure of the enzyme-ADT complex., Chang HJ, Shi R, Rehse P, Lin SX, J Biol Chem. 2004 Jan 23;279(4):2689-96. Epub 2003 Oct 21. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14573603 14573603]
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*[[Sulfotransferase 3D structures|Sulfotransferase 3D structures]]
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[[Category: Alcohol sulfotransferase]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Chang, H J.]]
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[[Category: Chang HJ]]
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[[Category: Lin, S X.]]
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[[Category: Lin SX]]
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[[Category: Rhese, P.]]
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[[Category: Rhese P]]
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[[Category: Shi, R.]]
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[[Category: Shi R]]
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[[Category: AE2]]
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[[Category: SO4]]
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[[Category: alpha/beta fold]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:15:59 2008''
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Current revision

Crystal structure of human DHEA-ST complexed with androsterone

PDB ID 1ov4

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