1fpq
From Proteopedia
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| - | [[Image:1fpq.jpg|left|200px]] | + | [[Image:1fpq.jpg|left|200px]] |
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| - | '''CRYSTAL STRUCTURE ANALYSIS OF SELENOMETHIONINE SUBSTITUTED CHALCONE O-METHYLTRANSFERASE''' | + | {{Structure |
| + | |PDB= 1fpq |SIZE=350|CAPTION= <scene name='initialview01'>1fpq</scene>, resolution 2.00Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''CRYSTAL STRUCTURE ANALYSIS OF SELENOMETHIONINE SUBSTITUTED CHALCONE O-METHYLTRANSFERASE''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1FPQ is a [ | + | 1FPQ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Medicago_sativa Medicago sativa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FPQ OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11224575 11224575] |
[[Category: Medicago sativa]] | [[Category: Medicago sativa]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: selenomethionine substituted protein]] | [[Category: selenomethionine substituted protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:12:21 2008'' |
Revision as of 09:12, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE ANALYSIS OF SELENOMETHIONINE SUBSTITUTED CHALCONE 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
1FPQ 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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