Diphthine synthase
From Proteopedia
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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== | ||
Revision as of 09:55, 25 February 2019
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3D structures of diphthine synthase
Updated on 25-February-2019
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 – PhDPS (mutant) + SAH – Pyrococcus horikoshii
1vce - PhDPS + SAH
3i4t - PhDPS (mutant) – Entamoeba histolytica
References
- ↑ Zhu X, Kim J, Su X, Lin H. Reconstitution of diphthine synthase activity in vitro. Biochemistry. 2010 Nov 9;49(44):9649-57. doi: 10.1021/bi100812h. PMID:20873788 doi:http://dx.doi.org/10.1021/bi100812h
