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1fpx
From Proteopedia
(New page: 200px<br /><applet load="1fpx" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fpx, resolution 1.65Å" /> '''CRYSTAL STRUCTURE AN...) |
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| - | [[Image:1fpx.jpg|left|200px]]<br /><applet load="1fpx" size=" | + | [[Image:1fpx.jpg|left|200px]]<br /><applet load="1fpx" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1fpx, resolution 1.65Å" /> | caption="1fpx, resolution 1.65Å" /> | ||
'''CRYSTAL STRUCTURE ANALYSIS OF SELENOMETHIONINE SUBSTITUTED ISOFLAVONE O-METHYLTRANSFERASE'''<br /> | '''CRYSTAL STRUCTURE ANALYSIS OF SELENOMETHIONINE SUBSTITUTED ISOFLAVONE O-METHYLTRANSFERASE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Chalcone O-methyltransferase (ChOMT) and isoflavone O-methyltransferase | + | Chalcone O-methyltransferase (ChOMT) and isoflavone O-methyltransferase (IOMT) are S-adenosyl-l-methionine (SAM) dependent plant natural product methyltransferases involved in secondary metabolism in Medicago sativa (alfalfa). Here we report the crystal structure of ChOMT in complex with the product S-adenosyl-l-homocysteine and the substrate isoliquiritigenin (4,2',4'-trihydroxychalcone) refined to 1.8 A as well as the crystal structure of IOMT in complex with the products S-adenosyl-l-homocysteine and isoformononetin (4'-hydroxy-7-methoxyisoflavone) refined to 1.4 A. These two OMTs constitute the first plant methyltransferases to be structurally characterized and reveal a novel oligomerization domain and the molecular determinants for substrate selection. As such, this work provides a structural basis for understanding the substrate specificity of the diverse family of plant OMTs and facilitates the engineering of novel activities in this extensive class of natural product biosynthetic enzymes. |
==About this Structure== | ==About this Structure== | ||
| - | 1FPX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Medicago_sativa Medicago sativa] with SAM as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1FPX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Medicago_sativa Medicago sativa] with <scene name='pdbligand=SAM:'>SAM</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FPX OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Medicago sativa]] | [[Category: Medicago sativa]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Dixon, R | + | [[Category: Dixon, R A.]] |
| - | [[Category: Noel, J | + | [[Category: Noel, J P.]] |
[[Category: Zubieta, C.]] | [[Category: Zubieta, C.]] | ||
[[Category: SAM]] | [[Category: SAM]] | ||
| Line 20: | Line 20: | ||
[[Category: selenomethionine]] | [[Category: selenomethionine]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:41:19 2008'' |
Revision as of 10:41, 21 February 2008
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CRYSTAL STRUCTURE ANALYSIS OF SELENOMETHIONINE SUBSTITUTED ISOFLAVONE O-METHYLTRANSFERASE
Overview
Chalcone O-methyltransferase (ChOMT) and isoflavone O-methyltransferase (IOMT) are S-adenosyl-l-methionine (SAM) dependent plant natural product methyltransferases involved in secondary metabolism in Medicago sativa (alfalfa). Here we report the crystal structure of ChOMT in complex with the product S-adenosyl-l-homocysteine and the substrate isoliquiritigenin (4,2',4'-trihydroxychalcone) refined to 1.8 A as well as the crystal structure of IOMT in complex with the products S-adenosyl-l-homocysteine and isoformononetin (4'-hydroxy-7-methoxyisoflavone) refined to 1.4 A. These two OMTs constitute the first plant methyltransferases to be structurally characterized and reveal a novel oligomerization domain and the molecular determinants for substrate selection. As such, this work provides a structural basis for understanding the substrate specificity of the diverse family of plant OMTs and facilitates the engineering of novel activities in this extensive class of natural product biosynthetic enzymes.
About this Structure
1FPX is a Single protein structure of sequence from Medicago sativa with as ligand. Full crystallographic information is available from OCA.
Reference
Structures of two natural product methyltransferases reveal the basis for substrate specificity in plant O-methyltransferases., Zubieta C, He XZ, Dixon RA, Noel JP, Nat Struct Biol. 2001 Mar;8(3):271-9. PMID:11224575
Page seeded by OCA on Thu Feb 21 12:41:19 2008
