Diphthine synthase
From Proteopedia
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| - | {{STRUCTURE_2dsi| PDB=2dsi | SIZE=400| SCENE= |right|CAPTION=Diphthine synthase complex with S-adenosyl-L-homocysteine [[2dsi]] }} | + | {{STRUCTURE_2dsi| PDB=2dsi | SIZE=400| SCENE= |right|CAPTION=Diphthine synthase complex with S-adenosyl-L-homocysteine, glycerol, MES and sulfate [[2dsi]] }} |
'''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. | ||
Revision as of 12:30, 1 January 2013
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.
3D structures of diphthine synthase
1vhv – DPS – Archaeoglobus fulgidus
2dsg, 2dsh, 2dsi, 2hr8, 2dv3, 2dv4, 2dv5, 2dv7, 2dxv, 2dxw, 2dxx, 2e07, 2e08, 2e15, 2e16, 2e17, 2e4n, 2e4r, 2e7r, 2ed3, 2ed5, 2eeq, 2owf, 2owg, 2owk, 2owu, 2owv, 2egb, 2z6r, 2egl, 2egs, 2eh2, 2eh4, 2eh5, 2ehc, 2ehl, 2ejj, 2ejk, 2p5c, 2p5f, 2p6d, 2p6i, 2p6k, 2ejz, 2ek2, 2ek3, 2ek4, 2ek7, 2eka, 2p6l, 2p9d, 2el0, 2el1, 2el2, 2el3, 2eld, 2ele, 2emr, 2emu, 2en5, 2eni, 2pb4, 2pb5, 2pb6, 2pca, 2pcg, 2pch, 2pci, 2pck, 2pcm – DPS (mutant) + SAH – Pyrococcus horikoshii
