1ps1

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[[Image:1ps1.jpg|left|200px]]
 
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==PENTALENENE SYNTHASE==
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The line below this paragraph, containing "STRUCTURE_1ps1", creates the "Structure Box" on the page.
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<StructureSection load='1ps1' size='340' side='right'caption='[[1ps1]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1ps1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_exfoliatus Streptomyces exfoliatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PS1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PS1 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 2.6&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PBM:TRIMETHYL+LEAD+ION'>PBM</scene></td></tr>
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{{STRUCTURE_1ps1| PDB=1ps1 | SCENE= }}
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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=1ps1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ps1 OCA], [https://pdbe.org/1ps1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ps1 RCSB], [https://www.ebi.ac.uk/pdbsum/1ps1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ps1 ProSAT]</span></td></tr>
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</table>
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'''PENTALENENE SYNTHASE'''
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== Function ==
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[https://www.uniprot.org/uniprot/PENA_STREX PENA_STREX] Catalyzes the cyclization of farnesyl diphosphate (FPP) to the tricyclic sesquiterpene pentalenene, which is the hydrocarbon precursor of the pentalenolactone family of antibiotics produced by a variety of Streptomyces species.<ref>PMID:8180213</ref>
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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/ps/1ps1_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1ps1 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 ==
The crystal structure of pentalenene synthase at 2.6 angstrom resolution reveals critical active site features responsible for the cyclization of farnesyl diphosphate into the tricyclic hydrocarbon pentalenene. Metal-triggered substrate ionization initiates catalysis, and the alpha-barrel active site serves as a template to channel and stabilize the conformations of reactive carbocation intermediates through a complex cyclization cascade. The core active site structure of the enzyme may be preserved among the greater family of terpenoid synthases, possibly implying divergence from a common ancestral synthase to satisfy biological requirements for increasingly diverse natural products.
The crystal structure of pentalenene synthase at 2.6 angstrom resolution reveals critical active site features responsible for the cyclization of farnesyl diphosphate into the tricyclic hydrocarbon pentalenene. Metal-triggered substrate ionization initiates catalysis, and the alpha-barrel active site serves as a template to channel and stabilize the conformations of reactive carbocation intermediates through a complex cyclization cascade. The core active site structure of the enzyme may be preserved among the greater family of terpenoid synthases, possibly implying divergence from a common ancestral synthase to satisfy biological requirements for increasingly diverse natural products.
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==About this Structure==
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Crystal structure of pentalenene synthase: mechanistic insights on terpenoid cyclization reactions in biology.,Lesburg CA, Zhai G, Cane DE, Christianson DW Science. 1997 Sep 19;277(5333):1820-4. PMID:9295272<ref>PMID:9295272</ref>
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1PS1 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_sp. Streptomyces sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PS1 OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Crystal structure of pentalenene synthase: mechanistic insights on terpenoid cyclization reactions in biology., Lesburg CA, Zhai G, Cane DE, Christianson DW, Science. 1997 Sep 19;277(5333):1820-4. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9295272 9295272]
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</div>
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[[Category: Pentalenene synthase]]
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<div class="pdbe-citations 1ps1" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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== References ==
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[[Category: Streptomyces sp.]]
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<references/>
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[[Category: Christianson, D W.]]
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__TOC__
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[[Category: Lesburg, C A.]]
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</StructureSection>
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[[Category: Antibiotic biosynthesis]]
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[[Category: Large Structures]]
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[[Category: Lyase]]
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[[Category: Streptomyces exfoliatus]]
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[[Category: Sesquiterpene cyclase]]
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[[Category: Christianson DW]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 05:25:15 2008''
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[[Category: Lesburg CA]]

Current revision

PENTALENENE SYNTHASE

PDB ID 1ps1

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