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4fr0

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==ArsM arsenic(III) S-adenosylmethionine methyltransferase with SAM==
==ArsM arsenic(III) S-adenosylmethionine methyltransferase with SAM==
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<StructureSection load='4fr0' size='340' side='right' caption='[[4fr0]], [[Resolution|resolution]] 2.75&Aring;' scene=''>
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<StructureSection load='4fr0' size='340' side='right'caption='[[4fr0]], [[Resolution|resolution]] 2.75&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4fr0]] 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=3qhu 3qhu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FR0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4FR0 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4fr0]] 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=3qhu 3qhu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FR0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FR0 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene></td></tr>
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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]] 2.75&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4fs8|4fs8]], [[4fsd|4fsd]]</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=SAM:S-ADENOSYLMETHIONINE'>SAM</scene></td></tr>
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<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>
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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=4fr0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fr0 OCA], [https://pdbe.org/4fr0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fr0 RCSB], [https://www.ebi.ac.uk/pdbsum/4fr0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fr0 ProSAT]</span></td></tr>
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<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=4fr0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fr0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4fr0 RCSB], [http://www.ebi.ac.uk/pdbsum/4fr0 PDBsum]</span></td></tr>
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</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/C0JV69_9RHOD C0JV69_9RHOD]
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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.
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Cyanidioschyzon sp. 5508]]
[[Category: Cyanidioschyzon sp. 5508]]
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[[Category: Ajees, A A]]
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[[Category: Large Structures]]
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[[Category: Marapakala, K]]
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[[Category: Ajees AA]]
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[[Category: Packianathan, C]]
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[[Category: Marapakala K]]
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[[Category: Rosen, B P]]
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[[Category: Packianathan C]]
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[[Category: Sankaran, B]]
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[[Category: Rosen BP]]
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[[Category: Arsenic methyltransferase]]
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[[Category: Sankaran B]]
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[[Category: Rossmann fold]]
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[[Category: Transferase]]
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Current revision

ArsM arsenic(III) S-adenosylmethionine methyltransferase with SAM

PDB ID 4fr0

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