Diphthine synthase

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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]] }}
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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.
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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>
==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 />
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== References ==
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<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Revision as of 13:55, 30 December 2015

Template:STRUCTURE 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.[1]

3D structures of diphthine synthase

Updated on 30-December-2015

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

  1. 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

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Michal Harel, Alexander Berchansky

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