1n22

From Proteopedia

(Difference between revisions)

Revision as of 08:07, 31 January 2018

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

Structural highlights

1n22 is a 2 chain structure with sequence from Salof. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, ,
Related:	1n1b, 1n1z, 1n20, 1n21, 1n23, 1n24
Activity:	(+)-bornyl diphosphate synthase, with EC number 5.5.1.8
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[BPPS_SALOF] Catalyzes the formation of the (+)-camphor precursor (+)-bornyl diphosphate from geranyl diphosphate. The enzyme also produces significant amounts of (+)-alpha-pinene, (+)-camphene, and (+-)-limonene.^[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Wise ML, Savage TJ, Katahira E, Croteau R. Monoterpene synthases from common sage (Salvia officinalis). cDNA isolation, characterization, and functional expression of (+)-sabinene synthase, 1,8-cineole synthase, and (+)-bornyl diphosphate synthase. J Biol Chem. 1998 Jun 12;273(24):14891-9. PMID:9614092
↑ Whittington DA, Wise ML, Urbansky M, Coates RM, Croteau RB, Christianson DW. Bornyl diphosphate synthase: structure and strategy for carbocation manipulation by a terpenoid cyclase. Proc Natl Acad Sci U S A. 2002 Nov 26;99(24):15375-80. Epub 2002 Nov 13. PMID:12432096 doi:10.1073/pnas.232591099

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1n22"

@@ Line 1: / Line 1: @@
 ==(+)-Bornyl Diphosphate Synthase: Complex with Mg, pyrophosphate, and (4R)-7-aza-7,8-dihydrolimonene==
 <StructureSection load='1n22' size='340' side='right' caption='[[1n22]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1n1b|1n1b]], [[1n1z|1n1z]], [[1n20|1n20]], [[1n21|1n21]], [[1n23|1n23]], [[1n24|1n24]]</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/(+)-bornyl_diphosphate_synthase (+)-bornyl diphosphate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.5.1.8 5.5.1.8] </span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1n22 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n22 OCA], [http://pdbe.org/1n22 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1n22 RCSB], [http://www.ebi.ac.uk/pdbsum/1n22 PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1n22 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n22 OCA], [http://pdbe.org/1n22 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1n22 RCSB], [http://www.ebi.ac.uk/pdbsum/1n22 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1n22 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 14: / Line 15: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/n2/1n22_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/n2/1n22_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>

1n22

From Proteopedia

Revision as of 08:07, 31 January 2018

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

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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