1n22

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(New page: 200px<br /><applet load="1n22" size="450" color="white" frame="true" align="right" spinBox="true" caption="1n22, resolution 2.40&Aring;" /> '''(+)-Bornyl Diphospha...)
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[[Image:1n22.gif|left|200px]]<br /><applet load="1n22" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1n22.gif|left|200px]]<br /><applet load="1n22" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1n22, resolution 2.40&Aring;" />
caption="1n22, resolution 2.40&Aring;" />
'''(+)-Bornyl Diphosphate Synthase: Complex with Mg, pyrophosphate, and (4R)-7-aza-7,8-dihydrolimonene'''<br />
'''(+)-Bornyl Diphosphate Synthase: Complex with Mg, pyrophosphate, and (4R)-7-aza-7,8-dihydrolimonene'''<br />
==Overview==
==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.
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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.
==About this Structure==
==About this Structure==
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1N22 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Salvia_officinalis Salvia officinalis] with MG, 7A8 and POP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Geranyl-diphosphate_cyclase Geranyl-diphosphate cyclase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.5.1.8 5.5.1.8] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1N22 OCA].
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1N22 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Salvia_officinalis Salvia officinalis] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=7A8:'>7A8</scene> and <scene name='pdbligand=POP:'>POP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Geranyl-diphosphate_cyclase Geranyl-diphosphate cyclase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.5.1.8 5.5.1.8] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N22 OCA].
==Reference==
==Reference==
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[[Category: Salvia officinalis]]
[[Category: Salvia officinalis]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Christianson, D.W.]]
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[[Category: Christianson, D W.]]
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[[Category: Coates, R.M.]]
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[[Category: Coates, R M.]]
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[[Category: Croteau, R.B.]]
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[[Category: Croteau, R B.]]
[[Category: Urbansky, M.]]
[[Category: Urbansky, M.]]
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[[Category: Whittington, D.A.]]
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[[Category: Whittington, D A.]]
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[[Category: Wise, M.L.]]
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[[Category: Wise, M L.]]
[[Category: 7A8]]
[[Category: 7A8]]
[[Category: MG]]
[[Category: MG]]
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[[Category: terpene synthase fold]]
[[Category: terpene synthase fold]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 21:52:59 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:01:23 2008''

Revision as of 12:01, 21 February 2008


1n22, resolution 2.40Å

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(+)-Bornyl Diphosphate Synthase: Complex with Mg, pyrophosphate, and (4R)-7-aza-7,8-dihydrolimonene

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.

About this Structure

1N22 is a Single protein structure of sequence from Salvia officinalis with , and as ligands. Active as Geranyl-diphosphate cyclase, with EC number 5.5.1.8 Full crystallographic information is available from OCA.

Reference

Bornyl diphosphate synthase: structure and strategy for carbocation manipulation by a terpenoid cyclase., Whittington DA, Wise ML, Urbansky M, Coates RM, Croteau RB, Christianson DW, Proc Natl Acad Sci U S A. 2002 Nov 26;99(24):15375-80. Epub 2002 Nov 13. PMID:12432096

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