Document Detail

Structures of two natural product methyltransferases reveal the basis for substrate specificity in plant O-methyltransferases.
MedLine Citation:
PMID:  11224575     Owner:  NLM     Status:  MEDLINE    
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.
C Zubieta; X Z He; R A Dixon; J P Noel
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Nature structural biology     Volume:  8     ISSN:  1072-8368     ISO Abbreviation:  Nat. Struct. Biol.     Publication Date:  2001 Mar 
Date Detail:
Created Date:  2001-03-06     Completed Date:  2001-03-29     Revised Date:  2009-11-19    
Medline Journal Info:
Nlm Unique ID:  9421566     Medline TA:  Nat Struct Biol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  271-9     Citation Subset:  IM    
Structural Biology Laboratory, The Salk Institute for Biological Studies, 10010 North Torrey Pines Road, La Jolla, California 92037, USA.
Data Bank Information
Bank Name/Acc. No.:
PDB/1FP1;  1FP2;  1FPQ;  1FPX
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MeSH Terms
Amino Acid Sequence
Binding Sites
Catechol O-Methyltransferase / chemistry
Chalcone / analogs & derivatives*,  metabolism
Chromatography, Thin Layer
Crystallography, X-Ray
DNA-Cytosine Methylases / chemistry
Histidine / genetics,  metabolism
Isoflavones / metabolism
Medicago sativa / enzymology*
Methyltransferases / chemistry*,  metabolism*
Models, Molecular
Molecular Sequence Data
Mutation / genetics
Protein Structure, Quaternary
Protein Structure, Tertiary
S-Adenosylhomocysteine / metabolism
Sequence Alignment
Substrate Specificity
Reg. No./Substance:
0/Chalcones; 0/Isoflavones; 71-00-1/Histidine; 94-41-7/Chalcone; 961-29-5/isoliquiritigenin; 979-92-0/S-Adenosylhomocysteine; EC 2.1.1.-/DNA modification methylase HhaI; EC 2.1.1.-/DNA-Cytosine Methylases; EC 2.1.1.-/Methyltransferases; EC O4'-methyltransferase; EC O-Methyltransferase

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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