3i4z
From Proteopedia
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| - | + | ==Crystal structure of the dimethylallyl tryptophan synthase FgaPT2 from Aspergillus fumigatus== | |
| - | === | + | <StructureSection load='3i4z' size='340' side='right' caption='[[3i4z]], [[Resolution|resolution]] 1.76Å' scene=''> |
| - | + | == Structural highlights == | |
| + | <table><tr><td colspan='2'>[[3i4z]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Aspergillus_fumigatus Aspergillus fumigatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3I4Z OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3I4Z FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BU2:1,3-BUTANEDIOL'>BU2</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3i4x|3i4x]]</td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/4-dimethylallyltryptophan_synthase 4-dimethylallyltryptophan synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.34 2.5.1.34] </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=3i4z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3i4z OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3i4z RCSB], [http://www.ebi.ac.uk/pdbsum/3i4z PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == 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/i4/3i4z_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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/chain_selection.php?pdb_ID=2ata ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Ergot alkaloids are toxins and important pharmaceuticals that are produced biotechnologically on an industrial scale. The first committed step of ergot alkaloid biosynthesis is catalyzed by dimethylallyl tryptophan synthase (DMATS; EC 2.5.1.34). Orthologs of DMATS are found in many fungal genomes. We report here the x-ray structure of DMATS, determined at a resolution of 1.76 A. A complex of DMATS from Aspergillus fumigatus with its aromatic substrate L-tryptophan and with an analogue of its isoprenoid substrate dimethylallyl diphosphate reveals the structural basis of this enzyme-catalyzed Friedel-Crafts reaction, which shows strict regiospecificity for position 4 of the indole nucleus of tryptophan as well as unusual independence of the presence of Mg(2+) ions. The 3D structure of DMATS belongs to a rare beta/alpha barrel fold, called prenyltransferase barrel, that was recently discovered in a small group of bacterial enzymes with no sequence similarity to DMATS. These bacterial enzymes catalyze the prenylation of aromatic substrates in the biosynthesis of secondary metabolites (i.e., a reaction similar to that of DMATS). | ||
| - | + | The structure of dimethylallyl tryptophan synthase reveals a common architecture of aromatic prenyltransferases in fungi and bacteria.,Metzger U, Schall C, Zocher G, Unsold I, Stec E, Li SM, Heide L, Stehle T Proc Natl Acad Sci U S A. 2009 Aug 25;106(34):14309-14. Epub 2009 Aug 12. PMID:19706516<ref>PMID:19706516</ref> | |
| - | + | ||
| - | == | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | < | + | </div> |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: 4-dimethylallyltryptophan synthase]] | [[Category: 4-dimethylallyltryptophan synthase]] | ||
[[Category: Aspergillus fumigatus]] | [[Category: Aspergillus fumigatus]] | ||
| - | [[Category: Schall, C | + | [[Category: Schall, C]] |
| - | [[Category: Stehle, T | + | [[Category: Stehle, T]] |
| - | [[Category: Zocher, G | + | [[Category: Zocher, G]] |
[[Category: Alkaloid metabolism]] | [[Category: Alkaloid metabolism]] | ||
[[Category: Prenyl transferase]] | [[Category: Prenyl transferase]] | ||
[[Category: Pt barrel]] | [[Category: Pt barrel]] | ||
[[Category: Transferase]] | [[Category: Transferase]] | ||
Revision as of 06:37, 18 December 2014
Crystal structure of the dimethylallyl tryptophan synthase FgaPT2 from Aspergillus fumigatus
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