+Search query
-Structure paper
Title | 3D architecture and structural flexibility revealed in the subfamily of large glutamate dehydrogenases by a mycobacterial enzyme. |
---|---|
Journal, issue, pages | Commun Biol, Vol. 4, Issue 1, Page 684, Year 2021 |
Publish date | Jun 3, 2021 |
Authors | Melisa Lázaro / Roberto Melero / Charlotte Huet / Jorge P López-Alonso / Sandra Delgado / Alexandra Dodu / Eduardo M Bruch / Luciano A Abriata / Pedro M Alzari / Mikel Valle / María-Natalia Lisa / |
PubMed Abstract | Glutamate dehydrogenases (GDHs) are widespread metabolic enzymes that play key roles in nitrogen homeostasis. Large glutamate dehydrogenases composed of 180 kDa subunits (L-GDHs) contain long N- ...Glutamate dehydrogenases (GDHs) are widespread metabolic enzymes that play key roles in nitrogen homeostasis. Large glutamate dehydrogenases composed of 180 kDa subunits (L-GDHs) contain long N- and C-terminal segments flanking the catalytic core. Despite the relevance of L-GDHs 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-GDH (mL-GDH) adopts a quaternary structure that is radically different from that of related low molecular weight enzymes. Intersubunit contacts in mL-GDH 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. |
External links | Commun Biol / PubMed:34083757 / PubMed Central |
Methods | EM (single particle) / X-ray diffraction |
Resolution | 3.59 - 6.6 Å |
Structure data | EMDB-11606, PDB-7a1d: EMDB-11612: EMDB-11613: PDB-7jsr: |
Source |
|
Keywords | OXIDOREDUCTASE / large glutamate dehydrogenase Mycobacterium metabolism / large glutamate dehydrogenase / Mycobacterium / metabolism |