1m6e

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(New page: 200px<br /><applet load="1m6e" size="450" color="white" frame="true" align="right" spinBox="true" caption="1m6e, resolution 3.00&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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[[Image:1m6e.jpg|left|200px]]<br /><applet load="1m6e" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1m6e, resolution 3.00&Aring;" />
 
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'''CRYSTAL STRUCTURE OF SALICYLIC ACID CARBOXYL METHYLTRANSFERASE (SAMT)'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE OF SALICYLIC ACID CARBOXYL METHYLTRANSFERASE (SAMT)==
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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.
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<StructureSection load='1m6e' size='340' side='right'caption='[[1m6e]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1m6e]] is a 1 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1M6E FirstGlance]. <br>
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1M6E is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Clarkia_breweri Clarkia breweri] with LU, SAH and SAL as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1M6E OCA].
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LU:LUTETIUM+(III)+ION'>LU</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>, <scene name='pdbligand=SAL:2-HYDROXYBENZOIC+ACID'>SAL</scene></td></tr>
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==Reference==
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1m6e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m6e OCA], [https://pdbe.org/1m6e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1m6e RCSB], [https://www.ebi.ac.uk/pdbsum/1m6e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1m6e ProSAT]</span></td></tr>
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=12897246 12897246]
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/SAMT_CLABR SAMT_CLABR] Catalyzes the methylation of the free carboxyl end of the plant hormone salicylic acid (SA). Converts SA to SA methyl ester (MSA). The volatile compound MSA is hypothesized to act as an airborne signal that triggers defense responses in uninfected plants. MSA is an important chemoattractant for moth pollinated flowering plants.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/m6/1m6e_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1m6e ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
[[Category: Clarkia breweri]]
[[Category: Clarkia breweri]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Koscheski, P.]]
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[[Category: Koscheski P]]
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[[Category: Noel, J.P.]]
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[[Category: Noel JP]]
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[[Category: Pichersky, E.]]
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[[Category: Pichersky E]]
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[[Category: Ross, J.R.]]
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[[Category: Ross JR]]
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[[Category: Yang, Y.]]
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[[Category: Yang Y]]
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[[Category: Zubieta, C.]]
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[[Category: Zubieta C]]
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[[Category: LU]]
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[[Category: SAH]]
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[[Category: SAL]]
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[[Category: protein-small molecule complex]]
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[[Category: rossmann fold]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 03:51:26 2007''
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Current revision

CRYSTAL STRUCTURE OF SALICYLIC ACID CARBOXYL METHYLTRANSFERASE (SAMT)

PDB ID 1m6e

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