View source for 7mfm


==Glutamate synthase, glutamate dehydrogenase counter-enzyme complex==
<StructureSection load='7mfm' size='340' side='right'caption='[[7mfm]], [[Resolution|resolution]] 2.42&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7mfm]] is a 10 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=7MFM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7MFM 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]] 2.42&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</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=7mfm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7mfm OCA], [https://pdbe.org/7mfm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7mfm RCSB], [https://www.ebi.ac.uk/pdbsum/7mfm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7mfm ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A0C3GZC9_BACIU A0A0C3GZC9_BACIU] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Multi-enzyme assemblies composed of metabolic enzymes catalyzing sequential reactions are being increasingly studied. Here, we report the discovery of a 1.6 megadalton multi-enzyme complex from Bacillus subtilis composed of two enzymes catalyzing opposite ('counter-enzymes') rather than sequential reactions: glutamate synthase (GltAB) and glutamate dehydrogenase (GudB), which make and break glutamate, respectively. In vivo and in vitro studies show that the primary role of complex formation is to inhibit the activity of GudB. Using cryo-electron microscopy, we elucidated the structure of the complex and the molecular basis of inhibition of GudB by GltAB. The complex exhibits unusual oscillatory progress curves and is necessary for both planktonic growth, in glutamate-limiting conditions, and for biofilm growth, in glutamate-rich media. The regulation of a key metabolic enzyme by complexing with its counter enzyme may thus enable cell growth under fluctuating glutamate concentrations.

A counter-enzyme complex regulates glutamate metabolism in Bacillus subtilis.,Jayaraman V, Lee DJ, Elad N, Vimer S, Sharon M, Fraser JS, Tawfik DS Nat Chem Biol. 2022 Feb;18(2):161-170. doi: 10.1038/s41589-021-00919-y. Epub 2021 , Dec 20. PMID:34931064<ref>PMID:34931064</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7mfm" style="background-color:#fffaf0;"></div>

==See Also==
*[[Glutamate dehydrogenase 3D structures|Glutamate dehydrogenase 3D structures]]
*[[Glutamate synthase|Glutamate synthase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bacillus subtilis]]
[[Category: Large Structures]]
[[Category: Elad N]]
[[Category: Fraser JS]]
[[Category: Jayaraman V]]
[[Category: Lee DJ]]
[[Category: Tawfik DS]]