3bd9
From Proteopedia
(Difference between revisions)
(New page: 200px<br /><applet load="3bd9" size="350" color="white" frame="true" align="right" spinBox="true" caption="3bd9, resolution 2.30Å" /> '''human 3-O-sulfotrans...) |
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| - | [[Image:3bd9.jpg|left|200px]]<br /><applet load="3bd9" size="350" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="3bd9, resolution 2.30Å" /> | ||
| - | '''human 3-O-sulfotransferase isoform 5 with bound PAP'''<br /> | ||
| - | == | + | ==human 3-O-sulfotransferase isoform 5 with bound PAP== |
| - | + | <StructureSection load='3bd9' size='340' side='right'caption='[[3bd9]], [[Resolution|resolution]] 2.30Å' scene=''> | |
| - | [[ | + | == Structural highlights == |
| - | + | <table><tr><td colspan='2'>[[3bd9]] 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=3BD9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BD9 FirstGlance]. <br> | |
| - | [ | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</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=3bd9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bd9 OCA], [https://pdbe.org/3bd9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3bd9 RCSB], [https://www.ebi.ac.uk/pdbsum/3bd9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3bd9 ProSAT]</span></td></tr> | |
| - | [ | + | </table> |
| - | [[ | + | == Function == |
| - | [ | + | [https://www.uniprot.org/uniprot/HS3S5_HUMAN HS3S5_HUMAN] Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) to catalyze the transfer of a sulfo group to position 3 of glucosamine residues in heparan. Catalyzes the rate limiting step in the biosynthesis of heparan sulfate (HSact). This modification is a crucial step in the biosynthesis of anticoagulant heparan sulfate as it completes the structure of the antithrombin pentasaccharide binding site. Also generates GlcUA-GlcNS or IdoUA-GlcNS and IdoUA2S-GlcNH2. The substrate-specific O-sulfation generates an enzyme-modified heparan sulfate which acts as a binding receptor to Herpes simplex virus-1 (HSV-1) and permits its entry.<ref>PMID:12138164</ref> |
| - | + | == Evolutionary Conservation == | |
| - | + | [[Image:Consurf_key_small.gif|200px|right]] | |
| - | + | Check<jmol> | |
| - | + | <jmolCheckbox> | |
| - | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bd/3bd9_consurf.spt"</scriptWhenChecked> | |
| - | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | |
| - | + | <text>to colour the structure by Evolutionary Conservation</text> | |
| - | + | </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/main_output.php?pdb_ID=3bd9 ConSurf]. | |
| - | + | <div style="clear:both"></div> | |
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The biosynthesis of heparan sulfate (HS) involves an array of specialized sulfotransferases. Here, we present a study aimed at engineering the substrate specificity of different HS 3-O-sulfotransferase isoforms. Based on the crystal structures, we identified a pair of amino acid residues responsible for selecting the substrates. Mutations of these residues altered the substrate specificities. Our results demonstrate the feasibility of tailoring the specificity of sulfotransferases to modify HS with desired functions. | ||
| - | + | Engineering sulfotransferases to modify heparan sulfate.,Xu D, Moon AF, Song D, Pedersen LC, Liu J Nat Chem Biol. 2008 Mar;4(3):200-2. Epub 2008 Jan 27. PMID:18223645<ref>PMID:18223645</ref> | |
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 3bd9" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Sulfotransferase 3D structures|Sulfotransferase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Liu J]] | ||
| + | [[Category: Moon AF]] | ||
| + | [[Category: Pedersen LC]] | ||
| + | [[Category: Song D]] | ||
| + | [[Category: Xu D]] | ||
Current revision
human 3-O-sulfotransferase isoform 5 with bound PAP
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Categories: Homo sapiens | Large Structures | Liu J | Moon AF | Pedersen LC | Song D | Xu D
