1fp2

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{{STRUCTURE_1fp2| PDB=1fp2 | SCENE= }}
{{STRUCTURE_1fp2| PDB=1fp2 | SCENE= }}
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'''CRYSTAL STRUCTURE ANALYSIS OF ISOFLAVONE O-METHYLTRANSFERASE'''
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===CRYSTAL STRUCTURE ANALYSIS OF ISOFLAVONE O-METHYLTRANSFERASE===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 11224575 is the PubMed ID number.
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{{ABSTRACT_PUBMED_11224575}}
==About this Structure==
==About this Structure==
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[[Category: Zubieta, C.]]
[[Category: Zubieta, C.]]
[[Category: Protein-product complex]]
[[Category: Protein-product complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:35:47 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 03:42:58 2008''

Revision as of 00:42, 1 July 2008

Image:1fp2.png

Template:STRUCTURE 1fp2

CRYSTAL STRUCTURE ANALYSIS OF ISOFLAVONE O-METHYLTRANSFERASE

Template:ABSTRACT PUBMED 11224575

About this Structure

1FP2 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

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