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 == | |||
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[[Category:Topic Page]] | [[Category:Topic Page]] |