1f1k: Difference between revisions

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 {{Theoretical_model}}
-{{Seed}}
-[[Image:1f1k.png|left|200px]]
-<!--
+==THEORETICAL MODEL OF THE ENZYME-PRODUCT COMPLEX OF ARISTOLOCHENE SYNTHASE==
-The line below this paragraph, containing "STRUCTURE_1f1k", creates the "Structure Box" on the page.
+<StructureSection load='1f1k' size='340' side='right'caption='[[1f1k]]' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1F1K FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</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=1f1k FirstGlance], [https://www.ebi.ac.uk/pdbsum/1f1k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1f1k ProSAT]</span></td></tr>
--->
+</table>
-{{STRUCTURE_1f1k|  PDB=1f1k  |  SCENE=  }}
+<div style="background-color:#fffaf0;">
+== 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.
-===THEORETICAL MODEL OF THE ENZYME-PRODUCT COMPLEX OF ARISTOLOCHENE SYNTHASE===
+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<ref>PMID:10825154</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-<!--
+</div>
-The line below this paragraph, {{ABSTRACT_PUBMED_10825154}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 1f1k" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 10825154 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_10825154}}
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Theoretical Model]]
-Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F1K OCA].
+[[Category: Large Structures]]
-==Reference==
-<ref group="xtra">PMID:10825154</ref><references group="xtra"/>
 [[Category: Cane, D E]]
 [[Category: Caruthers, J M]]
@@ Line 30: / Line 27: @@
 [[Category: Kang, I]]
 [[Category: Rynkiewicz, M J]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Apr  8 07:55:41 2010''