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<StructureSection load='7jsr' size='340' side='right'caption='[[7jsr]], [[Resolution|resolution]] 6.27&Aring;' scene=''>
<StructureSection load='7jsr' size='340' side='right'caption='[[7jsr]], [[Resolution|resolution]] 6.27&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[7jsr]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycs2 Mycs2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7JSR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7JSR FirstGlance]. <br>
<table><tr><td colspan='2'>[[7jsr]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycolicibacterium_smegmatis_MC2_155 Mycolicibacterium smegmatis MC2 155]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7JSR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7JSR FirstGlance]. <br>
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 6.27&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[7a1d|7a1d]]</div></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">gdh, MSMEG_4699, MSMEI_4582 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=246196 MYCS2])</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Glutamate_dehydrogenase Glutamate dehydrogenase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.1.2 1.4.1.2] </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=7jsr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7jsr OCA], [https://pdbe.org/7jsr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7jsr RCSB], [https://www.ebi.ac.uk/pdbsum/7jsr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7jsr 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=7jsr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7jsr OCA], [https://pdbe.org/7jsr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7jsr RCSB], [https://www.ebi.ac.uk/pdbsum/7jsr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7jsr ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/DHE2_MYCS2 DHE2_MYCS2]] Catalyzes the reversible conversion of L-glutamate to 2-oxoglutarate. Highly specific for NAD.<ref>PMID:19019160</ref>
[https://www.uniprot.org/uniprot/DHE2_MYCS2 DHE2_MYCS2] Catalyzes the reversible conversion of L-glutamate to 2-oxoglutarate. Highly specific for NAD.<ref>PMID:19019160</ref>  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Glutamate dehydrogenases (GDHs) are widespread metabolic enzymes that play key roles in nitrogen homeostasis. Large glutamate dehydrogenases composed of 180 kDa subunits (L-GDHs180) contain long N- and C-terminal segments flanking the catalytic core. Despite the relevance of L-GDHs180 in bacterial physiology, the lack of structural data for these enzymes has limited the progress of functional studies. Here we show that the mycobacterial L-GDH180 (mL-GDH180) adopts a quaternary structure that is radically different from that of related low molecular weight enzymes. Intersubunit contacts in mL-GDH180 involve a C-terminal domain that we propose as a new fold and a flexible N-terminal segment comprising ACT-like and PAS-type domains that could act as metabolic sensors for allosteric regulation. These findings uncover unique aspects of the structure-function relationship in the subfamily of L-GDHs.


3D architecture and structural flexibility revealed in the subfamily of large glutamate dehydrogenases by a mycobacterial enzyme.,Lazaro M, Melero R, Huet C, Lopez-Alonso JP, Delgado S, Dodu A, Bruch EM, Abriata LA, Alzari PM, Valle M, Lisa MN Commun Biol. 2021 Jun 3;4(1):684. doi: 10.1038/s42003-021-02222-x. PMID:34083757<ref>PMID:34083757</ref>
==See Also==
 
*[[Glutamate dehydrogenase 3D structures|Glutamate dehydrogenase 3D structures]]
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7jsr" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Glutamate dehydrogenase]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Mycs2]]
[[Category: Mycolicibacterium smegmatis MC2 155]]
[[Category: Abriata, L A]]
[[Category: Abriata LA]]
[[Category: Alzari, P M]]
[[Category: Alzari PM]]
[[Category: Bruch, E M]]
[[Category: Bruch EM]]
[[Category: Delgado, S]]
[[Category: Delgado S]]
[[Category: Dodu, A]]
[[Category: Dodu A]]
[[Category: Huet, C]]
[[Category: Huet C]]
[[Category: Lazaro, M]]
[[Category: Lazaro M]]
[[Category: Lisa, M N]]
[[Category: Lisa MN]]
[[Category: Lopez-Alonso, J P]]
[[Category: Lopez-Alonso JP]]
[[Category: Melero, R]]
[[Category: Melero R]]
[[Category: Valle, M]]
[[Category: Valle M]]
[[Category: Large glutamate dehydrogenase]]
[[Category: Metabolism]]
[[Category: Mycobacterium]]
[[Category: Oxidoreductase]]

Revision as of 07:16, 3 April 2024

Crystal structure of the large glutamate dehydrogenase composed of 180 kDa subunits from Mycobacterium smegmatis

7jsr, resolution 6.27Å

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