7a1d
From Proteopedia
(Difference between revisions)
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==Cryo-EM map of the large glutamate dehydrogenase composed of 180 kDa subunits from Mycobacterium smegmatis (open conformation)== | ==Cryo-EM map of the large glutamate dehydrogenase composed of 180 kDa subunits from Mycobacterium smegmatis (open conformation)== | ||
| - | <StructureSection load='7a1d' size='340' side='right'caption='[[7a1d]]' scene=''> | + | <StructureSection load='7a1d' size='340' side='right'caption='[[7a1d]], [[Resolution|resolution]] 4.19Å' 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=7A1D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7A1D FirstGlance]. <br> | + | <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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7a1d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7a1d OCA], [https://pdbe.org/7a1d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7a1d RCSB], [https://www.ebi.ac.uk/pdbsum/7a1d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7a1d ProSAT]</span></td></tr> | + | </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=7a1d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7a1d OCA], [https://pdbe.org/7a1d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7a1d RCSB], [https://www.ebi.ac.uk/pdbsum/7a1d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7a1d ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == 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> | ||
| + | <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> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7a1d" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Glutamate dehydrogenase 3D structures|Glutamate dehydrogenase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Glutamate dehydrogenase]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Abriata | + | [[Category: Mycs2]] |
| - | [[Category: Alzari | + | [[Category: Abriata, L A]] |
| - | [[Category: Bruch | + | [[Category: Alzari, P M]] |
| - | [[Category: Delgado S]] | + | [[Category: Bruch, E M]] |
| - | [[Category: Dodu A]] | + | [[Category: Delgado, S]] |
| - | [[Category: Huet C]] | + | [[Category: Dodu, A]] |
| - | [[Category: Lazaro M]] | + | [[Category: Huet, C]] |
| - | [[Category: Lisa | + | [[Category: Lazaro, M]] |
| - | [[Category: Lopez-Alonso | + | [[Category: Lisa, M N]] |
| - | [[Category: Melero R]] | + | [[Category: Lopez-Alonso, J P]] |
| - | [[Category: Valle M]] | + | [[Category: Melero, R]] |
| + | [[Category: Valle, M]] | ||
| + | [[Category: Large glutamate dehydrogenase mycobacterium metabolism]] | ||
| + | [[Category: Oxidoreductase]] | ||
Revision as of 05:49, 6 October 2021
Cryo-EM map of the large glutamate dehydrogenase composed of 180 kDa subunits from Mycobacterium smegmatis (open conformation)
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