1m6e
From Proteopedia
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| - | [[Image:1m6e.jpg|left|200px]] | + | [[Image:1m6e.jpg|left|200px]] |
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| - | '''CRYSTAL STRUCTURE OF SALICYLIC ACID CARBOXYL METHYLTRANSFERASE (SAMT)''' | + | {{Structure |
| + | |PDB= 1m6e |SIZE=350|CAPTION= <scene name='initialview01'>1m6e</scene>, resolution 3.00Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=LU:LUTETIUM+(III)+ION'>LU</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene> and <scene name='pdbligand=SAL:2-HYDROXYBENZOIC ACID'>SAL</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''CRYSTAL STRUCTURE OF SALICYLIC ACID CARBOXYL METHYLTRANSFERASE (SAMT)''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1M6E is a [ | + | 1M6E is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Clarkia_breweri Clarkia breweri]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M6E OCA]. |
==Reference== | ==Reference== | ||
| - | Structural basis for substrate recognition in the salicylic acid carboxyl methyltransferase family., Zubieta C, Ross JR, Koscheski P, Yang Y, Pichersky E, Noel JP, Plant Cell. 2003 Aug;15(8):1704-16. PMID:[http:// | + | Structural basis for substrate recognition in the salicylic acid carboxyl methyltransferase family., Zubieta C, Ross JR, Koscheski P, Yang Y, Pichersky E, Noel JP, Plant Cell. 2003 Aug;15(8):1704-16. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12897246 12897246] |
[[Category: Clarkia breweri]] | [[Category: Clarkia breweri]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: rossmann fold]] | [[Category: rossmann fold]] | ||
| - | ''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 12:39:32 2008'' |
Revision as of 10:39, 20 March 2008
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| , resolution 3.00Å | |||||||
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| Ligands: | , and | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF SALICYLIC ACID CARBOXYL METHYLTRANSFERASE (SAMT)
Overview
Recently, a novel family of methyltransferases was identified in plants. Some members of this newly discovered and recently characterized methyltransferase family catalyze the formation of small-molecule methyl esters using S-adenosyl-L-Met (SAM) as a methyl donor and carboxylic acid-bearing substrates as methyl acceptors. These enzymes include SAMT (SAM:salicylic acid carboxyl methyltransferase), BAMT (SAM:benzoic acid carboxyl methyltransferase), and JMT (SAM:jasmonic acid carboxyl methyltransferase). Moreover, other members of this family of plant methyltransferases have been found to catalyze the N-methylation of caffeine precursors. The 3.0-A crystal structure of Clarkia breweri SAMT in complex with the substrate salicylic acid and the demethylated product S-adenosyl-L-homocysteine reveals a protein structure that possesses a helical active site capping domain and a unique dimerization interface. In addition, the chemical determinants responsible for the selection of salicylic acid demonstrate the structural basis for facile variations of substrate selectivity among functionally characterized plant carboxyl-directed and nitrogen-directed methyltransferases and a growing set of related proteins that have yet to be examined biochemically. Using the three-dimensional structure of SAMT as a guide, we examined the substrate specificity of SAMT by site-directed mutagenesis and activity assays against 12 carboxyl-containing small molecules. Moreover, the utility of structural information for the functional characterization of this large family of plant methyltransferases was demonstrated by the discovery of an Arabidopsis methyltransferase that is specific for the carboxyl-bearing phytohormone indole-3-acetic acid.
About this Structure
1M6E is a Single protein structure of sequence from Clarkia breweri. Full crystallographic information is available from OCA.
Reference
Structural basis for substrate recognition in the salicylic acid carboxyl methyltransferase family., Zubieta C, Ross JR, Koscheski P, Yang Y, Pichersky E, Noel JP, Plant Cell. 2003 Aug;15(8):1704-16. PMID:12897246
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