1fpq: Difference between revisions

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[[Image:1fpq.jpg|left|200px]]
{{Seed}}
[[Image:1fpq.png|left|200px]]


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{{STRUCTURE_1fpq|  PDB=1fpq  |  SCENE=  }}  
{{STRUCTURE_1fpq|  PDB=1fpq  |  SCENE=  }}  


'''CRYSTAL STRUCTURE ANALYSIS OF SELENOMETHIONINE SUBSTITUTED CHALCONE O-METHYLTRANSFERASE'''
===CRYSTAL STRUCTURE ANALYSIS OF SELENOMETHIONINE SUBSTITUTED CHALCONE O-METHYLTRANSFERASE===




==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.
The line below this paragraph, {{ABSTRACT_PUBMED_11224575}}, adds the Publication Abstract to the page
(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: Selenomethionine substituted protein]]
[[Category: Selenomethionine substituted protein]]
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