1ps1: Difference between revisions

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[[Image:1ps1.jpg|left|200px]]
{{Seed}}
[[Image:1ps1.png|left|200px]]


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{{STRUCTURE_1ps1|  PDB=1ps1  |  SCENE=  }}  
{{STRUCTURE_1ps1|  PDB=1ps1  |  SCENE=  }}  


'''PENTALENENE SYNTHASE'''
===PENTALENENE SYNTHASE===




==Overview==
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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 line below this paragraph, {{ABSTRACT_PUBMED_9295272}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 9295272 is the PubMed ID number.
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{{ABSTRACT_PUBMED_9295272}}


==About this Structure==
==About this Structure==
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[[Category: Lyase]]
[[Category: Lyase]]
[[Category: Sesquiterpene cyclase]]
[[Category: Sesquiterpene cyclase]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 05:25:15 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 17:27:09 2008''

Revision as of 14:27, 27 July 2008

File:1ps1.png

Template:STRUCTURE 1ps1

PENTALENENE SYNTHASE

Template:ABSTRACT PUBMED 9295272

About this Structure

1PS1 is a Single protein structure of sequence from Streptomyces sp.. Full crystallographic information is available from OCA.

Reference

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

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