Diphthine synthase: Difference between revisions
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'''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> | '''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> | ||
<scene name='52/525183/Cv/ | <scene name='52/525183/Cv/5'>SAH binding site</scene>. | ||
<scene name='52/525183/Cv/ | <scene name='52/525183/Cv/6'>Na coordination site</scene> ([[2owu]]), water molecules shown as red spheres. | ||
</StructureSection> | </StructureSection> | ||
==3D structures of diphthine synthase== | ==3D structures of diphthine synthase== | ||