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1fpx

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[[Image:1fpx.jpg|left|200px]]
[[Image:1fpx.jpg|left|200px]]
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{{Structure
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|PDB= 1fpx |SIZE=350|CAPTION= <scene name='initialview01'>1fpx</scene>, resolution 1.65&Aring;
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The line below this paragraph, containing "STRUCTURE_1fpx", creates the "Structure Box" on the page.
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|SITE=
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|LIGAND= <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene>
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{{STRUCTURE_1fpx| PDB=1fpx | SCENE= }}
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|RELATEDENTRY=[[1fp1|1FP1]], [[1fp2|1FP2]], [[1fpq|1FPQ]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fpx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fpx OCA], [http://www.ebi.ac.uk/pdbsum/1fpx PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1fpx RCSB]</span>
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'''CRYSTAL STRUCTURE ANALYSIS OF SELENOMETHIONINE SUBSTITUTED ISOFLAVONE O-METHYLTRANSFERASE'''
'''CRYSTAL STRUCTURE ANALYSIS OF SELENOMETHIONINE SUBSTITUTED ISOFLAVONE O-METHYLTRANSFERASE'''
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[[Category: Noel, J P.]]
[[Category: Noel, J P.]]
[[Category: Zubieta, C.]]
[[Category: Zubieta, C.]]
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[[Category: s-adenosymethionine complex]]
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[[Category: S-adenosymethionine complex]]
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[[Category: selenomethionine]]
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[[Category: Selenomethionine]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:37:35 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:28:02 2008''
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Revision as of 13:37, 2 May 2008

Template:STRUCTURE 1fpx

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. 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 Fri May 2 16:37:35 2008

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