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Literature summary extracted from

  • Luo, M.; Singh, R.K.; Tanner, J.J.
    Structural determinants of oligomerization of delta(1)-pyrroline-5-carboxylate dehydrogenase: identification of a hexamerization hot spot (2013), J. Mol. Biol., 425, 3106-3120.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.2.1.88 expression in Escherichia coli Thermus thermophilus
1.2.1.88 expression in Escherichia coli Deinococcus radiodurans
1.2.1.88 expression in Escherichia coli Halalkalibacterium halodurans
1.2.1.88 expression in Escherichia coli Bacillus licheniformis

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.2.1.88
-
 Bacillus licheniformis
1.2.1.88 mutants R100A crystallizes in the same lattice as wild-type, mutant R100A/K104A/R111A crystaLLIZES IN space group P1 Thermus thermophilus
1.2.1.88 space group P21 with eight molecules in the asymmetric unit Halalkalibacterium halodurans

Protein Variants

EC Number Protein Variants Comment Organism
1.2.1.88 K104A mutation in alpha3 helix which participates in the dimer-dimer interaces. Catalytic efficiency similar to wild-type, mutant forms a hexamer Thermus thermophilus
1.2.1.88 R100A mutation in alpha3 helix which participates in the dimer-dimer interaces. Catalytic efficiency similar to wild-type, contrary to wild-type, the mutant forms a dimer Thermus thermophilus
1.2.1.88 R100A/K104A/R111A mutation in alpha3 helix which participates in the dimer-dimer interaces. Catalytic efficiency similar to wild-type, contrary to wild-type, the mutant forms a dimer Thermus thermophilus
1.2.1.88 R102A mutation in alpha3 helix which participates in the dimer-dimer interaces. Catalytic efficiency similar to wild-type, contrary to wild-type, the mutant forms a dimer Deinococcus radiodurans
1.2.1.88 R111A mutation in alpha3 helix which participates in the dimer-dimer interaces. Catalytic efficiency similar to wild-type, mutant forms a hexamer Thermus thermophilus
1.2.1.88 R153A mutation in alpha3 helix which participates in the dimer-dimer interaces. Catalytic efficiency similar to wild-type, mutant forms a hexamer Thermus thermophilus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.2.1.88 119000
-
 dynamic light scattering Halalkalibacterium halodurans
1.2.1.88 119000
-
 dynamic light scattering Bacillus licheniformis

Organism

EC Number Organism UniProt Comment Textmining
1.2.1.88 Bacillus licheniformis Q65NN2
-
-
1.2.1.88 Bacillus licheniformis DSM 13 Q65NN2
-
-
1.2.1.88 Deinococcus radiodurans Q9RW56
-
-
1.2.1.88 Deinococcus radiodurans DSM 20539 Q9RW56
-
-
1.2.1.88 Halalkalibacterium halodurans Q9K9B2
-
-
1.2.1.88 Halalkalibacterium halodurans DSM 18197 Q9K9B2
-
-
1.2.1.88 Thermus thermophilus Q72IB9
-
-
1.2.1.88 Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039 Q72IB9
-
-

Subunits

EC Number Subunits Comment Organism
1.2.1.88 dimer crystallization data Bacillus licheniformis
1.2.1.88 dimer dynamic light scattering and crystallization data Halalkalibacterium halodurans
1.2.1.88 hexamer protein exists primarily as a trimer-of-dimers hexamer in solution, small-angle X-ray scattering and crystallization data Thermus thermophilus
1.2.1.88 hexamer protein exists primarily as a trimer-of-dimers hexamer in solution, small-angle X-ray scattering and crystallization data Deinococcus radiodurans

Synonyms

EC Number Synonyms Comment Organism
1.2.1.88 DR_0813
-
 Deinococcus radiodurans