1n22

<StructureSection load='1n22' size='340' side='right' caption='[[1n22]], [[Resolution|resolution]] 2.40&Aring;' scene=''>

<table><tr><td colspan='2'>[[1n22]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Salof Salof]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N22 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1N22 FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=7A8:(1R)-DIMETHYL-(4-METHYL-CYCLOHEX-3-ENYL)-AMINE'>7A8</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=POP:PYROPHOSPHATE+2-'>POP</scene></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], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1n22 ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/BPPS_SALOF 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.<ref>PMID:9614092</ref>

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== 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<ref>PMID:12432096</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1n22" style="background-color:#fffaf0;"></div>

[[Category: Salof]]

[[Category: Christianson, D W]]

[[Category: Coates, R M]]

[[Category: Croteau, R B]]

[[Category: Urbansky, M]]

[[Category: Whittington, D A]]

[[Category: Wise, M L]]

[[Category: Isomerase]]

[[Category: Terpene synthase fold]]