7a1d

<table><tr><td colspan='2'>[[7a1d]] is a 4 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=7A1D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7A1D FirstGlance]. <br>

</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>

== 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>

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== 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>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 7a1d" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Glutamate dehydrogenase]]

[[Category: Abriata, L A]]

[[Category: Alzari, P M]]

[[Category: Bruch, E M]]

[[Category: Delgado, S]]

[[Category: Dodu, A]]

[[Category: Huet, C]]

[[Category: Lazaro, M]]

[[Category: Lisa, M N]]

[[Category: Lopez-Alonso, J P]]

[[Category: Melero, R]]

[[Category: Valle, M]]

[[Category: Oxidoreductase]]