Diphthine synthase: Difference between revisions
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<StructureSection load='2owu' size=' | <StructureSection load='2owu' size='450' side='right' scene='52/525183/Cv/1' 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.<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/2'>SAH binding site</scene>. | <scene name='52/525183/Cv/2'>SAH binding site</scene>. | ||
<scene name='52/525183/Cv/3'>Na coordination site</scene> ([[2owu]]), water molecules shown as red spheres. | |||
</StructureSection> | </StructureSection> | ||
==3D structures of diphthine synthase== | ==3D structures of diphthine synthase== | ||