Diphthine synthase: Difference between revisions

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{{STRUCTURE_2dsi|  PDB=2dsi | SIZE=400| SCENE= |right|CAPTION=Diphthine synthase complex with S-adenosyl-L-homocysteine, glycerol, MES and sulfate [[2dsi]] }}
{{STRUCTURE_2owu|  PDB=2owu | SIZE=400| SCENE= |right|CAPTION=Diphthine synthase complex with S-adenosyl-L-homocysteine, glycerol, MES and sulfate [[2owu]] }}


'''Diphthine synthase''' (DPS) is a S-adenosyl-L-methionine (SAM)-dependent methyltransferase.  DPS catalyzes the trimethylation of a specific histidine residue in elongation factor 2 forming a diphthine and producing S-adenosyl-L-homocysteine (SAH).  DPS participates in the diphthamide biosynthesis.
'''Diphthine synthase''' (DPS) is a S-adenosyl-L-methionine (SAM)-dependent methyltransferase.  DPS catalyzes the trimethylation of a specific histidine residue in elongation factor 2 forming a diphthine and producing S-adenosyl-L-homocysteine (SAH).  DPS participates in the diphthamide biosynthesis.

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Michal Harel, Alexander Berchansky