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Title3D architecture and structural flexibility revealed in the subfamily of large glutamate dehydrogenases by a mycobacterial enzyme.
Journal, issue, pagesCommun Biol, Vol. 4, Issue 1, Page 684, Year 2021
Publish dateJun 3, 2021
AuthorsMelisa 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 AbstractGlutamate 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 linksCommun Biol / PubMed:34083757 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution3.59 - 6.6 Å
Structure data

11606

7a1d

EMDB-11606, PDB-7a1d:
Cryo-EM map of the large glutamate dehydrogenase composed of 180 kDa subunits from Mycobacterium smegmatis (open conformation)
Method: EM (single particle) / Resolution: 4.19 Å

EMDB-11612:
Cryo-EM map of the large glutamate dehydrogenase composed of 180 kDa subunits from Mycobacterium smegmatis (close conformation)
Method: EM (single particle) / Resolution: 6.6 Å

EMDB-11613:
Cryo-EM map of the large glutamate dehydrogenase composed of 180 kDa subunits from Mycobacterium smegmatis (monomer)
Method: EM (single particle) / Resolution: 3.59 Å

PDB-7jsr:
Crystal structure of the large glutamate dehydrogenase composed of 180 kDa subunits from Mycobacterium smegmatis
Method: X-RAY DIFFRACTION / Resolution: 6.27 Å

Source
  • Mycolicibacterium smegmatis MC2 155 (bacteria)
  • mycolicibacterium smegmatis (strain atcc 700084 / mc(2)155) (bacteria)
  • mycolicibacterium smegmatis (bacteria)
KeywordsOXIDOREDUCTASE / large glutamate dehydrogenase Mycobacterium metabolism / large glutamate dehydrogenase / Mycobacterium / metabolism

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