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==The structure of an As(III) S-adenosylmethionine methyltransferase: insights into the mechanism of arsenic biotransformation==
==The structure of an As(III) S-adenosylmethionine methyltransferase: insights into the mechanism of arsenic biotransformation==
<StructureSection load='4fs8' size='340' side='right' caption='[[4fs8]], [[Resolution|resolution]] 1.78&Aring;' scene=''>
<StructureSection load='4fs8' size='340' side='right'caption='[[4fs8]], [[Resolution|resolution]] 1.78&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4fs8]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Cyanidioschyzon_sp._5508 Cyanidioschyzon sp. 5508]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3p7e 3p7e]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FS8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4FS8 FirstGlance]. <br>
<table><tr><td colspan='2'>[[4fs8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Cyanidioschyzon_sp._5508 Cyanidioschyzon sp. 5508]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3p7e 3p7e]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FS8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FS8 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.78&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4fr0|4fr0]], [[4fsd|4fsd]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">arsM ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=610260 Cyanidioschyzon sp. 5508])</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=4fs8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fs8 OCA], [https://pdbe.org/4fs8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fs8 RCSB], [https://www.ebi.ac.uk/pdbsum/4fs8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fs8 ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4fs8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fs8 OCA], [http://pdbe.org/4fs8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4fs8 RCSB], [http://www.ebi.ac.uk/pdbsum/4fs8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4fs8 ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Function ==
== Publication Abstract from PubMed ==
[https://www.uniprot.org/uniprot/C0JV69_9RHOD C0JV69_9RHOD]
Enzymatic methylation of arsenic is a detoxification process in microorganisms but in humans may activate the metalloid to more carcinogenic species. We describe the first structure of an As(III) S-adenosylmethionine methyltransferase by X-ray crystallography that reveals a novel As(III) binding domain. The structure of the methyltransferase from the thermophilic eukaryotic alga Cyanidioschyzon merolae reveals the relationship between the arsenic and S-adenosylmethionine binding sites to a final resolution of approximately 1.6 A. As(III) binding causes little change in conformation, but binding of SAM reorients helix alpha4 and a loop (residues 49-80) toward the As(III) binding domain, positioning the methyl group for transfer to the metalloid. There is no evidence of a reductase domain. These results are consistent with previous suggestions that arsenic remains trivalent during the catalytic cycle. A homology model of human As(III) S-adenosylmethionine methyltransferase with the location of known polymorphisms was constructed. The structure provides insights into the mechanism of substrate binding and catalysis.
 
Structure of an As(III) S-Adenosylmethionine Methyltransferase: Insights into the Mechanism of Arsenic Biotransformation.,Ajees AA, Marapakala K, Packianathan C, Sankaran B, Rosen BP Biochemistry. 2012 Jun 29. PMID:22712827<ref>PMID:22712827</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4fs8" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Cyanidioschyzon sp. 5508]]
[[Category: Cyanidioschyzon sp. 5508]]
[[Category: Ajees, A A]]
[[Category: Large Structures]]
[[Category: Marapakala, K]]
[[Category: Ajees AA]]
[[Category: Packianathan, C]]
[[Category: Marapakala K]]
[[Category: Rosen, B P]]
[[Category: Packianathan C]]
[[Category: Sankaran, B]]
[[Category: Rosen BP]]
[[Category: Arsenic methyltransferase]]
[[Category: Sankaran B]]
[[Category: Rossmann fold]]
[[Category: Transferase]]
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