8gf5: Difference between revisions

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<table><tr><td colspan='2'>[[8gf5]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanosarcina_acetivorans_C2A Methanosarcina acetivorans C2A]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8GF5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8GF5 FirstGlance]. <br>
<table><tr><td colspan='2'>[[8gf5]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanosarcina_acetivorans_C2A Methanosarcina acetivorans C2A]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8GF5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8GF5 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3&#8491;</td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AGM:5-METHYL-ARGININE'>AGM</scene>, <scene name='pdbligand=COM:1-THIOETHANESULFONIC+ACID'>COM</scene>, <scene name='pdbligand=F43:FACTOR+430'>F43</scene>, <scene name='pdbligand=MHS:N1-METHYLATED+HISTIDINE'>MHS</scene>, <scene name='pdbligand=SMC:S-METHYLCYSTEINE'>SMC</scene>, <scene name='pdbligand=TP7:COENZYME+B'>TP7</scene></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AGM:5-METHYL-ARGININE'>AGM</scene>, <scene name='pdbligand=COM:1-THIOETHANESULFONIC+ACID'>COM</scene>, <scene name='pdbligand=MHS:N1-METHYLATED+HISTIDINE'>MHS</scene>, <scene name='pdbligand=SMC:S-METHYLCYSTEINE'>SMC</scene>, <scene name='pdbligand=TP7:COENZYME+B'>TP7</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=8gf5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8gf5 OCA], [https://pdbe.org/8gf5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8gf5 RCSB], [https://www.ebi.ac.uk/pdbsum/8gf5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8gf5 ProSAT]</span></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=8gf5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8gf5 OCA], [https://pdbe.org/8gf5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8gf5 RCSB], [https://www.ebi.ac.uk/pdbsum/8gf5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8gf5 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[https://www.uniprot.org/uniprot/MCRA_METAC MCRA_METAC] Component of the methyl-coenzyme M reductase (MCR) I that catalyzes the reductive cleavage of methyl-coenzyme M (CoM-S-CH3 or 2-(methylthio)ethanesulfonate) using coenzyme B (CoB or 7-mercaptoheptanoylthreonine phosphate) as reductant which results in the production of methane and the mixed heterodisulfide of CoB and CoM (CoM-S-S-CoB). This is the final step in methanogenesis.[UniProtKB:P11558]
[https://www.uniprot.org/uniprot/Q8THH0_METAC Q8THH0_METAC]  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Methyl-coenzyme M reductase (MCR) catalyzes the formation of methane, and its activity accounts for nearly all biologically produced methane released into the atmosphere. The assembly of MCR is an intricate process involving the installation of a complex set of posttranslational modifications and the unique Ni-containing tetrapyrrole called coenzyme F(430). Despite decades of research, details of MCR assembly remain largely unresolved. Here, we report the structural characterization of MCR in two intermediate states of assembly. These intermediate states lack one or both F(430) cofactors and form complexes with the previously uncharacterized McrD protein. McrD is found to bind asymmetrically to MCR, displacing large regions of the alpha subunit and increasing active-site accessibility for the installation of F(430)-shedding light on the assembly of MCR and the role of McrD therein. This work offers crucial information for the expression of MCR in a heterologous host and provides targets for the design of MCR inhibitors.
 
McrD binds asymmetrically to methyl-coenzyme M reductase improving active-site accessibility during assembly.,Chadwick GL, Joiner AMN, Ramesh S, Mitchell DA, Nayak DD Proc Natl Acad Sci U S A. 2023 Jun 20;120(25):e2302815120. doi: , 10.1073/pnas.2302815120. Epub 2023 Jun 12. PMID:37307484<ref>PMID:37307484</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8gf5" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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Retrieved from "https://proteopedia.org/8gf5"