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==== | ==Glutamate synthase, glutamate dehydrogenase counter-enzyme complex (GudB6-GltA6-GltB6)== | ||
<StructureSection load='7mft' size='340' side='right'caption='[[7mft]]' scene=''> | <StructureSection load='7mft' size='340' side='right'caption='[[7mft]], [[Resolution|resolution]] 3.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id= OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol= FirstGlance]. <br> | <table><tr><td colspan='2'>[[7mft]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis_subsp._subtilis_NCIB_3610_=_ATCC_6051_=_DSM_10 Bacillus subtilis subsp. subtilis NCIB 3610 = ATCC 6051 = DSM 10]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7MFT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7MFT FirstGlance]. <br> | ||
</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=7mft FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7mft OCA], [https://pdbe.org/7mft PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7mft RCSB], [https://www.ebi.ac.uk/pdbsum/7mft PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7mft ProSAT]</span></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]] 3.9Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=F3S:FE3-S4+CLUSTER'>F3S</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</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=7mft FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7mft OCA], [https://pdbe.org/7mft PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7mft RCSB], [https://www.ebi.ac.uk/pdbsum/7mft PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7mft ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/GUDB_BACSU GUDB_BACSU] GudB seems to be intrinsically inactive, however spontaneous mutations removing a 9-bp direct repeat within the wild-type gudB sequence activated the GudB protein and allowed more-efficient utilization of amino acids of the glutamate family. This insertion presumably causes severe destabilization of the fold of the protein, leading to an inactive enzyme that is very quickly degraded. The cryptic GudB serves as a buffer that may compensate for mutations in the rocG gene and that can also be decryptified for the utilization of glutamate as a single carbon source in the absence of arginine. It is unable to synthesize glutamate.<ref>PMID:9829940</ref> <ref>PMID:18326565</ref> | |||
<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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7mft" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Glutamate dehydrogenase 3D structures|Glutamate dehydrogenase 3D structures]] | |||
*[[Glutamate synthase|Glutamate synthase]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Bacillus subtilis subsp. subtilis NCIB 3610 = ATCC 6051 = DSM 10]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Elad N]] | ||
[[Category: Fraser JS]] | |||
[[Category: Jayaraman V]] | |||
[[Category: Lee DJ]] | |||
[[Category: Tawfik DS]] | |||