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1ps1

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{{STRUCTURE_1ps1| PDB=1ps1 | SCENE= }}
{{STRUCTURE_1ps1| PDB=1ps1 | SCENE= }}
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'''PENTALENENE SYNTHASE'''
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===PENTALENENE SYNTHASE===
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==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.
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(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]]
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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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''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

Image: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

Page seeded by OCA on Sun Jul 27 17:27:09 2008

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