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| | <StructureSection load='1di1' size='340' side='right'caption='[[1di1]], [[Resolution|resolution]] 2.50Å' scene=''> | | <StructureSection load='1di1' size='340' side='right'caption='[[1di1]], [[Resolution|resolution]] 2.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1di1]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_10110 Atcc 10110]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DI1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1DI1 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1di1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_10110 Atcc 10110]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DI1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DI1 FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1dgp|1dgp]], [[1f1l|1f1l]], [[1f1k|1f1k]], [[1f1n|1f1n]], [[1f1p|1f1p]]</td></tr> | + | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1dgp|1dgp]], [[1f1l|1f1l]], [[1f1k|1f1k]], [[1f1n|1f1n]], [[1f1p|1f1p]]</div></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Aristolochene_synthase Aristolochene synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.3.9 4.2.3.9] </span></td></tr> | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Aristolochene_synthase Aristolochene synthase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.3.9 4.2.3.9] </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=1di1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1di1 OCA], [http://pdbe.org/1di1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1di1 RCSB], [http://www.ebi.ac.uk/pdbsum/1di1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1di1 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=1di1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1di1 OCA], [https://pdbe.org/1di1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1di1 RCSB], [https://www.ebi.ac.uk/pdbsum/1di1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1di1 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/ARIS_PENRO ARIS_PENRO]] Catalyzes the cyclization of trans,trans-farnesyl diphosphate (FPP) to the bicyclic sesquiterpene aristolochene. Produces germacrene A as an enzyme-bound intermediate that is not released by the enzyme, but is further cyclized to produce aristolochene. Aristolochene is the likely parent compound for a number of sesquiterpenoid toxins produced by filamentous fungi.<ref>PMID:8440737</ref> <ref>PMID:15186158</ref> | + | [[https://www.uniprot.org/uniprot/ARIS_PENRO ARIS_PENRO]] Catalyzes the cyclization of trans,trans-farnesyl diphosphate (FPP) to the bicyclic sesquiterpene aristolochene. Produces germacrene A as an enzyme-bound intermediate that is not released by the enzyme, but is further cyclized to produce aristolochene. Aristolochene is the likely parent compound for a number of sesquiterpenoid toxins produced by filamentous fungi.<ref>PMID:8440737</ref> <ref>PMID:15186158</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| Structural highlights
Function
[ARIS_PENRO] Catalyzes the cyclization of trans,trans-farnesyl diphosphate (FPP) to the bicyclic sesquiterpene aristolochene. Produces germacrene A as an enzyme-bound intermediate that is not released by the enzyme, but is further cyclized to produce aristolochene. Aristolochene is the likely parent compound for a number of sesquiterpenoid toxins produced by filamentous fungi.[1] [2]
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 PubMed
The 2.5-A resolution crystal structure of recombinant aristolochene synthase from the blue cheese mold, Penicillium roqueforti, is the first of a fungal terpenoid cyclase. The structure of the enzyme reveals active site features that participate in the cyclization of the universal sesquiterpene cyclase substrate, farnesyl diphosphate, to form the bicyclic hydrocarbon aristolochene. Metal-triggered carbocation formation initiates the cyclization cascade, which proceeds through multiple complex intermediates to yield one exclusive structural and stereochemical isomer of aristolochene. Structural homology of this fungal cyclase with plant and bacterial terpenoid cyclases, despite minimal amino acid sequence identity, suggests divergence from a common, primordial ancestor in the evolution of terpene biosynthesis.
Crystal structure determination of aristolochene synthase from the blue cheese mold, Penicillium roqueforti.,Caruthers JM, Kang I, Rynkiewicz MJ, Cane DE, Christianson DW J Biol Chem. 2000 Aug 18;275(33):25533-9. PMID:10825154[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Proctor RH, Hohn TM. Aristolochene synthase. Isolation, characterization, and bacterial expression of a sesquiterpenoid biosynthetic gene (Ari1) from Penicillium roqueforti. J Biol Chem. 1993 Feb 25;268(6):4543-8. PMID:8440737
- ↑ Felicetti B, Cane DE. Aristolochene synthase: mechanistic analysis of active site residues by site-directed mutagenesis. J Am Chem Soc. 2004 Jun 16;126(23):7212-21. PMID:15186158 doi:10.1021/ja0499593
- ↑ Caruthers JM, Kang I, Rynkiewicz MJ, Cane DE, Christianson DW. Crystal structure determination of aristolochene synthase from the blue cheese mold, Penicillium roqueforti. J Biol Chem. 2000 Aug 18;275(33):25533-9. PMID:10825154 doi:10.1074/jbc.M000433200
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