1ps1: Difference between revisions

Line 1:

[[Image:1ps1.~~jpg~~|left|200px]]

[[Image:1ps1.png|left|200px]]

<!--

Line 9:

Line 10:

~~'''~~PENTALENENE SYNTHASE~~'''~~

===PENTALENENE SYNTHASE===

~~==Overview==~~

<!--

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.

-->

==About this Structure==

Line 28:

Line 32:

[[Category: Lyase]]

[[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''

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 1: / Line 1: @@
-[[Image:1ps1.jpg|left|200px]]
+{{Seed}}
+[[Image:1ps1.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1ps1|  PDB=1ps1  |  SCENE=  }}
-'''PENTALENENE SYNTHASE'''
+===PENTALENENE SYNTHASE===
-==Overview==
+<!--
-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.
+-->
+{{ABSTRACT_PUBMED_9295272}}
 ==About this Structure==
@@ Line 28: / Line 32: @@
 [[Category: Lyase]]
 [[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''