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{{STRUCTURE_3lcc|  PDB=3lcc  |  SCENE=  }}
===Structure of a SAM-dependent halide methyltransferase from Arabidopsis thaliana===


==Function==
==Structure of a SAM-dependent halide methyltransferase from Arabidopsis thaliana==
[[http://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>
<StructureSection load='3lcc' size='340' side='right'caption='[[3lcc]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
<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'>[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>
== 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 ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <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>
    <text>to colour the structure by Evolutionary Conservation</text>
  </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/main_output.php?pdb_ID=3lcc ConSurf].
<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.


==About this Structure==
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>
[[3lcc]] is a 1 chain structure with sequence from [http://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].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
<ref group="xtra">PMID:020376845</ref><references group="xtra"/><references/>
</div>
<div class="pdbe-citations 3lcc" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Arabidopsis thaliana]]
[[Category: Arabidopsis thaliana]]
[[Category: Hagan, D O.]]
[[Category: Large Structures]]
[[Category: Naismith, J H.]]
[[Category: Naismith JH]]
[[Category: Schmidberger, J W.]]
[[Category: O'Hagan D]]
[[Category: Halide methyltransferase]]
[[Category: Schmidberger JW]]
[[Category: Transferase]]

Latest revision as of 16:22, 1 November 2023

Structure of a SAM-dependent halide methyltransferase from Arabidopsis thaliana

3lcc, resolution 1.80Å

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