1fp2
From Proteopedia
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|PDB= 1fp2 |SIZE=350|CAPTION= <scene name='initialview01'>1fp2</scene>, resolution 1.40Å | |PDB= 1fp2 |SIZE=350|CAPTION= <scene name='initialview01'>1fp2</scene>, resolution 1.40Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=HMO:4'-HYDROXY-7-METHOXYISOFLAVONE'>HMO</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1fp1|1FP1]], [[1fpx|1FPX]], [[1fpq|1FPQ]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fp2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fp2 OCA], [http://www.ebi.ac.uk/pdbsum/1fp2 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1fp2 RCSB]</span> | ||
}} | }} | ||
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[[Category: Noel, J P.]] | [[Category: Noel, J P.]] | ||
[[Category: Zubieta, C.]] | [[Category: Zubieta, C.]] | ||
| - | [[Category: HMO]] | ||
| - | [[Category: SAH]] | ||
[[Category: protein-product complex]] | [[Category: protein-product complex]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:27:21 2008'' |
Revision as of 17:27, 30 March 2008
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| , resolution 1.40Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Related: | 1FP1, 1FPX, 1FPQ
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE ANALYSIS OF ISOFLAVONE O-METHYLTRANSFERASE
Overview
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.
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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