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TitleTertiary and quaternary structure remodeling by occupancy of the substrate binding pocket in a large glutamate dehydrogenase
Journal, issue, pagesTo Be Published
Publish dateDec 23, 2024 (structure data deposition date)
AuthorsLazaro M / Chamorro N / Lopez-Alonso JP / Charro D / Rasia RM / Jimenez-Oses G / Valle M / Lisa MN
External linksSearch PubMed
MethodsEM (single particle)
Resolution2.63 - 4.1 Å
Structure data

52419

9hux

EMDB-52419: CryoEM map of the large glutamate dehydrogenase composed of 180 kDa subunits from Mycobacterium smegmatis obtained in the presence of NAD+ and L-glutamate. Open Tetramer
PDB-9hux: CryoEM map of the large glutamate dehydrogenase composed of 180 kDa subunits from Mycobacterium smegmatis obtained in the presence of NAD+ and L-glutamate. Open Tetramer.
Method: EM (single particle) / Resolution: 3.88 Å

52420

9huy

EMDB-52420, PDB-9huy:
CryoEM map of the large glutamate dehydrogenase composed of 180 kDa subunits from Mycobacterium smegmatis obtained in the presence of NAD+ and L-glutamate. Closed1 tetramer.
Method: EM (single particle) / Resolution: 3.54 Å

52421

9huz

EMDB-52421, PDB-9huz:
CryoEM map of the large glutamate dehydrogenase composed of 180 kDa subunits from Mycobacterium smegmatis obtained in the presence of NAD+ and L-glutamate. Closed2 tetramer
Method: EM (single particle) / Resolution: 3.57 Å

52422

9hv0

EMDB-52422, PDB-9hv0:
CryoEM map of the large glutamate dehydrogenase composed of 180 kDa subunits from Mycobacterium smegmatis obtained in the presence of NAD+ and L-glutamate. Empty monomer.
Method: EM (single particle) / Resolution: 3.07 Å

52423

9hv4

EMDB-52423, PDB-9hv4:
CryoEM map of the large glutamate dehydrogenase composed of 180 kDa subunits from Mycobacterium smegmatis obtained in the presence of NAD+ and L-glutamate. cofactor-monomer.
Method: EM (single particle) / Resolution: 2.95 Å

52424

9hv5

EMDB-52424, PDB-9hv5:
CryoEM map of the large glutamate dehydrogenase composed of 180 kDa subunits from Mycobacterium smegmatis obtained in the presence of NAD+ and L-glutamate. Cofactor/ligand-monomer
Method: EM (single particle) / Resolution: 3.12 Å

EMDB-52425: CryoEM map of the large glutamate dehydrogenase composed of 180 kDa subunits from Mycobacterium smegmatis obtained in the presence of NAD+ and L-glutamate. cofactor/ligand-monomer in Open tetramer.
Method: EM (single particle) / Resolution: 3.23 Å

EMDB-52426: CryoEM map of the large glutamate dehydrogenase composed of 180 kDa subunits from Mycobacterium smegmatis obtained in the presence of NAD+ and L-glutamate. cofactor/ligand-monomer in Closed1 tetramer.
Method: EM (single particle) / Resolution: 3.11 Å

EMDB-52427: CryoEM map of the large glutamate dehydrogenase composed of 180 kDa subunits from Mycobacterium smegmatis obtained in the presence of NAD+ and L-glutamate. cofactor/ligand-monomer in Closed2 tetramer.
Method: EM (single particle) / Resolution: 3.18 Å

52428

9hv6

EMDB-52428, PDB-9hv6:
CryoEM map of the large glutamate dehydrogenase composed of 180 kDa subunits from Mycobacterium smegmatis obtained in the presence of NAD+ and L-glutamate. Total-monomer
Method: EM (single particle) / Resolution: 2.63 Å

EMDB-52429: CryoEM map of the large glutamate dehydrogenase composed of 180 kDa subunits from Mycobacterium smegmatis obtained in the presence of NAD+ and L-glutamate. Closed2 tetramer with cofactor/ligand-monomer.
Method: EM (single particle) / Resolution: 4.1 Å

Chemicals

ChemComp-NAD:
NICOTINAMIDE-ADENINE-DINUCLEOTIDE / NAD*YM

ChemComp-GLU:
GLUTAMIC ACID

Source
  • mycolicibacterium smegmatis (bacteria)
KeywordsOXIDOREDUCTASE / Large glutamate dehydrogenase / Tetramer

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