1f1k: Difference between revisions
New page: '''Theoretical Model''' The entry 1F1K is a Theoretical Model titled 'THEORETICAL MODEL OF THE ENZYME-PRODUCT COMPLEX OF ARISTOLOCHENE SYNTHASE'. Category:Theoretical Model ''Page ... |
No edit summary |
||
| (10 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
{{Theoretical_model}} | |||
==THEORETICAL MODEL OF THE ENZYME-PRODUCT COMPLEX OF ARISTOLOCHENE SYNTHASE== | |||
<StructureSection load='1f1k' size='340' side='right'caption='[[1f1k]]' scene=''> | |||
== Structural highlights == | |||
<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> | |||
</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> | |||
<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. | |||
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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1f1k" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Theoretical Model]] | |||
[[Category: Large Structures]] | |||
[[Category: Cane, D E]] | |||
[[Category: Caruthers, J M]] | |||
[[Category: Christianson, D W]] | |||
[[Category: Kang, I]] | |||
[[Category: Rynkiewicz, M J]] | |||
Latest revision as of 12:45, 21 July 2021
 |
THEORETICAL MODEL OF THE ENZYME-PRODUCT COMPLEX OF ARISTOLOCHENE SYNTHASETHEORETICAL MODEL OF THE ENZYME-PRODUCT COMPLEX OF ARISTOLOCHENE SYNTHASE
Structural highlights
Publication Abstract from PubMedThe 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
| ||||||||||||||