2j5c: Difference between revisions
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[[Image:2j5c.gif|left|200px]]<br /><applet load="2j5c" size=" | [[Image:2j5c.gif|left|200px]]<br /><applet load="2j5c" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="2j5c, resolution 1.95Å" /> | caption="2j5c, resolution 1.95Å" /> | ||
'''RATIONAL CONVERSION OF SUBSTRATE AND PRODUCT SPECIFICITY IN A MONOTERPENE SYNTHASE. STRUCTURAL INSIGHTS INTO THE MOLECULAR BASIS OF RAPID EVOLUTION.'''<br /> | '''RATIONAL CONVERSION OF SUBSTRATE AND PRODUCT SPECIFICITY IN A MONOTERPENE SYNTHASE. STRUCTURAL INSIGHTS INTO THE MOLECULAR BASIS OF RAPID EVOLUTION.'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
2J5C is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Salvia_fruticosa Salvia fruticosa] with BME as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Site: <scene name='pdbsite=AC1:Bme Binding Site For Chain B'>AC1</scene>. Full crystallographic information is available from [http:// | 2J5C is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Salvia_fruticosa Salvia fruticosa] with <scene name='pdbligand=BME:'>BME</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Site: <scene name='pdbsite=AC1:Bme Binding Site For Chain B'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J5C OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: terpene synthases]] | [[Category: terpene synthases]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 14:06:43 2008'' | ||
Revision as of 15:06, 23 January 2008
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RATIONAL CONVERSION OF SUBSTRATE AND PRODUCT SPECIFICITY IN A MONOTERPENE SYNTHASE. STRUCTURAL INSIGHTS INTO THE MOLECULAR BASIS OF RAPID EVOLUTION.
OverviewOverview
Terpene synthases are responsible for the biosynthesis of the complex, chemical defense arsenal of plants and microorganisms. How do these, enzymes, which all appear to share a common terpene synthase fold, specify, the many different products made almost entirely from one of only three, substrates? Elucidation of the structure of 1,8-cineole synthase from, Salvia fruticosa (Sf-CinS1) combined with analysis of functional and, phylogenetic relationships of enzymes within Salvia species identified, active-site residues responsible for product specificity. Thus, Sf-CinS1, was successfully converted to a sabinene synthase with a minimum number of, rationally predicted substitutions, while identification of the Asn side, chain essential for water activation introduced 1,8-cineole and, alpha-terpineol activity to Salvia pomifera sabinene synthase. A major, contribution to product specificity in Sf-CinS1 appears to come from a, local deformation within one of the helices forming the active site. This, deformation is observed in all other mono- or sesquiterpene structures, available, pointing to a conserved mechanism. Moreover, a single amino, acid substitution enlarged the active-site cavity enough to accommodate, the larger farnesyl pyrophosphate substrate and led to the efficient, synthesis of sesquiterpenes, while alternate single substitutions of this, critical amino acid yielded five additional terpene synthases.
About this StructureAbout this Structure
2J5C is a Single protein structure of sequence from Salvia fruticosa with as ligand. Known structural/functional Site: . Full crystallographic information is available from OCA.
ReferenceReference
Rational Conversion of Substrate and Product Specificity in a Salvia Monoterpene Synthase: Structural Insights into the Evolution of Terpene Synthase Function., Kampranis SC, Ioannidis D, Purvis A, Mahrez W, Ninga E, Katerelos NA, Anssour S, Dunwell JM, Degenhardt J, Makris AM, Goodenough PW, Johnson CB, Plant Cell. 2007 Jun 8;. PMID:17557809
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