Diphthine synthase: Difference between revisions

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{{STRUCTURE_2owu|  PDB=2owu  | SIZE=400| SCENE= |right|CAPTION=Diphthine synthase complex with S-adenosyl-L-homocysteine (SAH) and Na+ ion [[2owu]] }}
{{STRUCTURE_2owu|  PDB=2owu  | SIZE=400| SCENE= |right|CAPTION=Diphthine synthase complex with S-adenosyl-L-homocysteine (SAH) and Na+ ion [[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.<ref>PMID:20873788</ref>


==3D structures of diphthine synthase==
==3D structures of diphthine synthase==
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[[1vce]] - PhDPS + SAH<br />
[[1vce]] - PhDPS + SAH<br />
[[3i4t]] - PhDPS (mutant) – ''Entamoeba histolytica''<br />
[[3i4t]] - PhDPS (mutant) – ''Entamoeba histolytica''<br />
 
== References ==
<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

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Michal Harel, Alexander Berchansky