7qbv
From Proteopedia
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==B12-dependent radical SAM methyltransferase, Mmp10 with [4Fe-4S] cluster, cobalamin, and S-adenosyl-L-homocysteine bound.== | ==B12-dependent radical SAM methyltransferase, Mmp10 with [4Fe-4S] cluster, cobalamin, and S-adenosyl-L-homocysteine bound.== | ||
| - | <StructureSection load='7qbv' size='340' side='right'caption='[[7qbv]]' scene=''> | + | <StructureSection load='7qbv' size='340' side='right'caption='[[7qbv]], [[Resolution|resolution]] 2.70Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7QBV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7QBV FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7qbv]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanosarcina_acetivorans Methanosarcina acetivorans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7QBV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7QBV FirstGlance]. <br> |
| - | </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=7qbv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7qbv OCA], [https://pdbe.org/7qbv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7qbv RCSB], [https://www.ebi.ac.uk/pdbsum/7qbv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7qbv ProSAT]</span></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]] 2.701Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=COB:CO-METHYLCOBALAMIN'>COB</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</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=7qbv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7qbv OCA], [https://pdbe.org/7qbv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7qbv RCSB], [https://www.ebi.ac.uk/pdbsum/7qbv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7qbv ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/MCRAM_METAC MCRAM_METAC] Radical SAM methyltransferase that is responsible for the C(5)-methylation of 'Arg-285' of the methyl-coenzyme M reductase (MCR) subunit alpha McrA. This post-translational methylation, despite being not essential in vivo, plays a role for the stability and structural integrity of MCR.<ref>PMID:29743535</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | By catalysing the microbial formation of methane, methyl-coenzyme M reductase has a central role in the global levels of this greenhouse gas(1,2). The activity of methyl-coenzyme M reductase is profoundly affected by several unique post-translational modifications(3-6), such as a unique C-methylation reaction catalysed by methanogenesis marker protein 10 (Mmp10), a radical S-adenosyl-L-methionine (SAM) enzyme(7,8). Here we report the spectroscopic investigation and atomic resolution structure of Mmp10 from Methanosarcina acetivorans, a unique B12 (cobalamin)-dependent radical SAM enzyme(9). The structure of Mmp10 reveals a unique enzyme architecture with four metallic centres and critical structural features involved in the control of catalysis. In addition, the structure of the enzyme-substrate complex offers a glimpse into a B12-dependent radical SAM enzyme in a precatalytic state. By combining electron paramagnetic resonance spectroscopy, structural biology and biochemistry, our study illuminates the mechanism by which the emerging superfamily of B12-dependent radical SAM enzymes catalyse chemically challenging alkylation reactions and identifies distinctive active site rearrangements to provide a structural rationale for the dual use of the SAM cofactor for radical and nucleophilic chemistry. | ||
| + | |||
| + | Crystallographic snapshots of a B12-dependent radical SAM methyltransferase.,Fyfe CD, Bernardo-Garcia N, Fradale L, Grimaldi S, Guillot A, Brewee C, Chavas LMG, Legrand P, Benjdia A, Berteau O Nature. 2022 Feb;602(7896):336-342. doi: 10.1038/s41586-021-04355-9. Epub 2022, Feb 2. PMID:35110733<ref>PMID:35110733</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7qbv" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| + | [[Category: Methanosarcina acetivorans]] | ||
[[Category: Benjdia A]] | [[Category: Benjdia A]] | ||
[[Category: Berteau O]] | [[Category: Berteau O]] | ||
Current revision
B12-dependent radical SAM methyltransferase, Mmp10 with [4Fe-4S] cluster, cobalamin, and S-adenosyl-L-homocysteine bound.
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