View source for 9gzq


==Structure of ForCE lacking the Helical Membrane Plug-in (HMP; DUF1641)==
<StructureSection load='9gzq' size='340' side='right'caption='[[9gzq]], [[Resolution|resolution]] 3.63&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9gzq]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9GZQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9GZQ 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]] 3.626&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=4MO:MOLYBDENUM(IV)+ION'>4MO</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=MGD:2-AMINO-5,6-DIMERCAPTO-7-METHYL-3,7,8A,9-TETRAHYDRO-8-OXA-1,3,9,10-TETRAAZA-ANTHRACEN-4-ONE+GUANOSINE+DINUCLEOTIDE'>MGD</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=9gzq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9gzq OCA], [https://pdbe.org/9gzq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9gzq RCSB], [https://www.ebi.ac.uk/pdbsum/9gzq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9gzq ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/YJGC_BACSU YJGC_BACSU] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Redox processes are at the heart of energetic metabolism that drives life on earth. By extension, complex and efficient electron transfer wires are necessary to connect the various metabolic pathways that are often located in distinct cellular compartments. Here, we uncovered a structural module that enables channeling of quinones from the membrane to various water-soluble redox catalytic units in prokaryotes. Using X-ray crystallography and cryo-electron microscopy, we determined the structure of the unusual bacterial formate dehydrogenase ForCE that contains four ForC catalytic subunits docked around a membrane-associated tetrameric ForE central scaffold. In the latter, a conserved domain that we propose to name helical membrane plugin (HMP) was identified as essential to link formate oxidation, in Bacillus subtilis, to the aerobic respiratory chain. Our bioinformatic analysis indicates that this HMP is associated with different quinone-reducing oxidoreductases, highlighting its broad importance as a functional unit to wire electrons between a given catalytic redox center and the quinone pool.

A scaffold for quinone channeling between membrane and soluble bacterial oxidoreductases.,Broc M, Cherrier MV, Uzel A, Arias-Cartin R, Arnoux P, Brasseur G, Seduk F, Guigliarelli B, Legrand P, Pierrel F, Schoehn G, Mate MJ, Martin L, Grimaldi S, Nicolet Y, Magalon A, Walburger A Nat Struct Mol Biol. 2025 Aug 25. doi: 10.1038/s41594-025-01607-4. PMID:40855134<ref>PMID:40855134</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 9gzq" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bacillus subtilis]]
[[Category: Large Structures]]
[[Category: Arias-Cartin R]]
[[Category: Arnoux P]]
[[Category: Broc M]]
[[Category: Cherrier MV]]
[[Category: Legrand P]]
[[Category: Magalon A]]
[[Category: Nicolet Y]]
[[Category: Seduk F]]
[[Category: Walburger A]]