7qbu

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==B12-dependent radical SAM methyltransferase, Mmp10 with [4Fe-4S] cluster, cobalamin, and S-methyl-5'-thioadenosine bound.==
==B12-dependent radical SAM methyltransferase, Mmp10 with [4Fe-4S] cluster, cobalamin, and S-methyl-5'-thioadenosine bound.==
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<StructureSection load='7qbu' size='340' side='right'caption='[[7qbu]]' scene=''>
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<StructureSection load='7qbu' size='340' side='right'caption='[[7qbu]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7QBU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7QBU FirstGlance]. <br>
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<table><tr><td colspan='2'>[[7qbu]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7QBU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7QBU FirstGlance]. <br>
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</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=7qbu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7qbu OCA], [https://pdbe.org/7qbu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7qbu RCSB], [https://www.ebi.ac.uk/pdbsum/7qbu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7qbu ProSAT]</span></td></tr>
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</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=MTA:5-DEOXY-5-METHYLTHIOADENOSINE'>MTA</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></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=7qbu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7qbu OCA], [https://pdbe.org/7qbu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7qbu RCSB], [https://www.ebi.ac.uk/pdbsum/7qbu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7qbu ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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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>
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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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<div class="pdbe-citations 7qbu" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Benjdia A]]
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[[Category: Benjdia, A]]
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[[Category: Berteau O]]
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[[Category: Berteau, O]]
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[[Category: Chavas LMG]]
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[[Category: Chavas, L M.G]]
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[[Category: Fyfe CD]]
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[[Category: Fyfe, C D]]
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[[Category: Legrand P]]
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[[Category: Legrand, P]]
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[[Category: B12 binding]]
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[[Category: Metal binding protein]]
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[[Category: Methyltransferase]]
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[[Category: Radical sam]]
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[[Category: Sp3 carbon methylation]]

Revision as of 11:08, 16 February 2022

B12-dependent radical SAM methyltransferase, Mmp10 with [4Fe-4S] cluster, cobalamin, and S-methyl-5'-thioadenosine bound.

PDB ID 7qbu

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