1FPQ

CRYSTAL STRUCTURE ANALYSIS OF SELENOMETHIONINE SUBSTITUTED CHALCONE O-METHYLTRANSFERASE

Summary for 1FPQ

• Entry DOI: 10.2210/pdb1fpq/pdb
• Related: 1FP1 1FP2 1FPX
• Descriptor: ISOLIQUIRITIGENIN 2'-O-METHYLTRANSFERASE, S-ADENOSYLMETHIONINE (3 entities in total)
• Functional Keywords: selenomethionine substituted protein, transferase
• Biological source: Medicago sativa
• Total number of polymer chains: 1
• Total formula weight: 42280.01

Authors

Zubieta, C.,Dixon, R.A.,Noel, J.P. (deposition date: 2000-08-31, release date: 2001-03-07, Last modification date: 2024-11-13)

Primary citation

Zubieta, C.,He, X.Z.,Dixon, R.A.,Noel, J.P.
Structures of two natural product methyltransferases reveal the basis for substrate specificity in plant O-methyltransferases.
Nat.Struct.Biol., 8:271-279, 2001

PubMed Abstract: 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.

PubMed: 11224575
DOI: 10.1038/85029

Experimental method

X-RAY DIFFRACTION (2 Å)