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3lcc
From Proteopedia
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==Structure of a SAM-dependent halide methyltransferase from Arabidopsis thaliana== | ==Structure of a SAM-dependent halide methyltransferase from Arabidopsis thaliana== | ||
| - | <StructureSection load='3lcc' size='340' side='right' caption='[[3lcc]], [[Resolution|resolution]] 1.80Å' scene=''> | + | <StructureSection load='3lcc' size='340' side='right'caption='[[3lcc]], [[Resolution|resolution]] 1.80Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3lcc]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[3lcc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LCC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3LCC FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8Å</td></tr> |
| - | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3lcc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lcc OCA], [https://pdbe.org/3lcc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3lcc RCSB], [https://www.ebi.ac.uk/pdbsum/3lcc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3lcc ProSAT]</span></td></tr> |
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/HOL1_ARATH HOL1_ARATH] S-adenosyl-L-methionine-dependent methyltransferase. Involved in glucosinolate metabolism and defense against phytopathogens. Highly reactive to thiocyanate (NCS(-)) derived from myrosinase-mediated hydrolysis of glucosinolates upon tissue damage.[REFERENCE:8]<ref>PMID:19419967</ref> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/lc/3lcc_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/lc/3lcc_consurf.spt"</scriptWhenChecked> |
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
| - | </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/ | + | </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=3lcc ConSurf]. |
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | A product structure of the halomethane producing enzyme in plants (Arabidopsis thaliana) is reported and a model for presentation of chloride/bromide ion to the methyl group of S-adenosyl-L-methionine (SAM) is presented to rationalise nucleophilic halide attack for halomethane production, gaseous natural products that are produced globally. | ||
| + | |||
| + | Halomethane biosynthesis: structure of a SAM-dependent halide methyltransferase from Arabidopsis thaliana.,Schmidberger JW, James AB, Edwards R, Naismith JH, O'Hagan D Angew Chem Int Ed Engl. 2010 May 10;49(21):3646-8. doi: 10.1002/anie.201000119. PMID:20376845<ref>PMID:20376845</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 3lcc" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Arabidopsis thaliana]] | [[Category: Arabidopsis thaliana]] | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: Naismith | + | [[Category: Naismith JH]] |
| - | [[Category: | + | [[Category: O'Hagan D]] |
| - | [[Category: | + | [[Category: Schmidberger JW]] |
| - | + | ||
Current revision
Structure of a SAM-dependent halide methyltransferase from Arabidopsis thaliana
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