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    
Abstract/OtherAbstract:
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.
Authors:
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    
Affiliation:
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
Descriptor/Qualifier:
Amino Acid Sequence
Binding Sites
Catechol O-Methyltransferase / chemistry
Chalcone / analogs & derivatives*,  metabolism
Chalcones
Chromatography, Thin Layer
Crystallography, X-Ray
DNA-Cytosine Methylases / chemistry
Dimerization
Histidine / genetics,  metabolism
Hydroxylation
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
Chemical
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 2.1.1.46/isoflavone O4'-methyltransferase; EC 2.1.1.6/Catechol O-Methyltransferase

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


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