8w33
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of McrD (methyl-coenzyme M reductase operon protein D) from Methanomassiliicoccus luminyensis== | |
| + | <StructureSection load='8w33' size='340' side='right'caption='[[8w33]], [[Resolution|resolution]] 1.65Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[8w33]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanomassiliicoccus_luminyensis_B10 Methanomassiliicoccus luminyensis B10]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8W33 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8W33 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]] 1.65Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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=8w33 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8w33 OCA], [https://pdbe.org/8w33 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8w33 RCSB], [https://www.ebi.ac.uk/pdbsum/8w33 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8w33 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Methyl-coenzyme M reductase (MCR) is a multi-subunit (alpha(2)beta(2)gamma(2)) enzyme responsible for methane formation via its unique F(430) cofactor. The genes responsible for producing MCR (mcrA, mcrB and mcrG) are typically colocated with two other highly conserved genes mcrC and mcrD. We present here the high-resolution crystal structure for McrD from a human gut methanogen Methanomassiliicoccus luminyensis strain B10. The structure reveals that McrD comprises a ferredoxin-like domain assembled into an alpha + beta barrel-like dimer with conformational flexibility exhibited by a functional loop. The description of the M. luminyensis McrD crystal structure contributes to our understanding of this key conserved methanogen protein typically responsible for promoting MCR activity and the production of methane, a greenhouse gas. | ||
| - | + | The crystal structure of methanogen McrD, a methyl-coenzyme M reductase-associated protein.,Sutherland-Smith AJ, Carbone V, Schofield LR, Cronin B, Duin EC, Ronimus RS FEBS Open Bio. 2024 Jun 14. doi: 10.1002/2211-5463.13848. PMID:38877345<ref>PMID:38877345</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 8w33" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Methanomassiliicoccus luminyensis B10]] | ||
| + | [[Category: Carbone V]] | ||
| + | [[Category: Ronimus RS]] | ||
| + | [[Category: Schofield LR]] | ||
| + | [[Category: Sutherland-Smith AJ]] | ||
Current revision
Structure of McrD (methyl-coenzyme M reductase operon protein D) from Methanomassiliicoccus luminyensis
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