1n23: Difference between revisions

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[[Image:1n23.~~gif~~|left|200px]]

[[Image:1n23.png|left|200px]]

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~~'''~~(+)-Bornyl diphosphate synthase: Complex with Mg, pyrophosphate, and (1R,4S)-2-azabornane~~'''~~

===(+)-Bornyl diphosphate synthase: Complex with Mg, pyrophosphate, and (1R,4S)-2-azabornane===

~~==Overview==~~

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The ~~x-ray crystal structure of dimeric (+)-bornyl diphosphate synthase~~, ~~a metal-requiring monoterpene cyclase from Salvia officinalis~~, ~~is reported~~ at 2.~~0-A resolution~~. ~~Each monomer contains two alpha-helical domains: the C-terminal domain catalyzes the cyclization of geranyl diphosphate~~, ~~orienting and stabilizing multiple reactive carbocation intermediates;~~ the N-~~terminal domain has no clearly defined function, although its N terminus caps the active site in the C~~-terminal domain during catalysis. Structures of complexes with aza analogues of substrate and carbocation intermediates, as well as complexes with pyrophosphate and bornyl diphosphate, provide "snapshots" of the terpene cyclization cascade.

The line below this paragraph, {{ABSTRACT_PUBMED_12432096}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 12432096 is the PubMed ID number.

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==About this Structure==

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[[Category: Wise, M L.]]

[[Category: Terpene synthase fold]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sat May 3 01~~:59:35 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 19:48:31 2008''

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-[[Image:1n23.gif|left|200px]]
+{{Seed}}
+[[Image:1n23.png|left|200px]]
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 {{STRUCTURE_1n23|  PDB=1n23  |  SCENE=  }}
-'''(+)-Bornyl diphosphate synthase: Complex with Mg, pyrophosphate, and (1R,4S)-2-azabornane'''
+===(+)-Bornyl diphosphate synthase: Complex with Mg, pyrophosphate, and (1R,4S)-2-azabornane===
-==Overview==
+<!--
-The x-ray crystal structure of dimeric (+)-bornyl diphosphate synthase, a metal-requiring monoterpene cyclase from Salvia officinalis, is reported at 2.0-A resolution. Each monomer contains two alpha-helical domains: the C-terminal domain catalyzes the cyclization of geranyl diphosphate, orienting and stabilizing multiple reactive carbocation intermediates; the N-terminal domain has no clearly defined function, although its N terminus caps the active site in the C-terminal domain during catalysis. Structures of complexes with aza analogues of substrate and carbocation intermediates, as well as complexes with pyrophosphate and bornyl diphosphate, provide "snapshots" of the terpene cyclization cascade.
+The line below this paragraph, {{ABSTRACT_PUBMED_12432096}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12432096 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_12432096}}
 ==About this Structure==
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 [[Category: Wise, M L.]]
 [[Category: Terpene synthase fold]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 01:59:35 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 19:48:31 2008''