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Literature summary for 2.1.1.98 extracted from

  • Kishishita, S.; Shimizu, K.; Murayama, K.; Terada, T.; Shirouzu, M.; Yokoyama, S.; Kunishima, N.
    Structures of two archaeal diphthine synthases: insights into the post-translational modification of elongation factor 2 (2008), Acta Crystallogr. Sect. D, 64, 397-406.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging-drop vapour-diffusion method at 20°C, structure is resolved at 2.0 A resolution. The homodimeric crystal structures of the archaeal diphthine synthases from Pyrococcus horikoshii DSM 12428 and Aeropyrum pernix DSM 11879 share the same overall fold as the cobalt-precorrin-4 methyltransferase CbiF Aeropyrum pernix
microbatch method, structure is resolved at 2.1 A resolution. The homodimeric crystal structures of the archaeal diphthine synthases from Pyrococcus horikoshii DSM 12428 and Aeropyrum pernix DSM 11879share the same overall fold as the cobalt-precorrin-4 methyltransferase CbiF Pyrococcus horikoshii

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
29600
-
2 * 29600, calculated from sequence, crystallographic data, only one of the two active sites binds the reaction product S-adenosyl-L-homocysteine, while the other active site contains no ligand Pyrococcus horikoshii
31500
-
2 * 31500, calculated from sequence, crystallographic data, only one of the two active sites binds the reaction product S-adenosyl-L-homocysteine, while the other active site contains no ligand Aeropyrum pernix

Organism

Organism UniProt Comment Textmining
Aeropyrum pernix Q9YDI2
-
-
Aeropyrum pernix DSM 11879 Q9YDI2
-
-
Pyrococcus horikoshii O58456
-
-
Pyrococcus horikoshii DSM 12428 O58456
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Aeropyrum pernix
-
Pyrococcus horikoshii

Subunits

Subunits Comment Organism
dimer 2 * 29600, calculated from sequence, crystallographic data, only one of the two active sites binds the reaction product S-adenosyl-L-homocysteine, while the other active site contains no ligand Pyrococcus horikoshii
dimer 2 * 31500, calculated from sequence, crystallographic data, only one of the two active sites binds the reaction product S-adenosyl-L-homocysteine, while the other active site contains no ligand Aeropyrum pernix

Synonyms

Synonyms Comment Organism
Dph5
-
Aeropyrum pernix
Dph5
-
Pyrococcus horikoshii