Diphthine synthase

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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>
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<scene name='52/525183/Cv/2'>SAH binding site</scene>.
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<scene name='52/525183/Cv/5'>SAH binding site</scene>.
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<scene name='52/525183/Cv/3'>Na coordination site</scene> ([[2owu]]), water molecules shown as red spheres.
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<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==
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[[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''<br />
[[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''<br />
[[1vce]] - PhDPS + SAH<br />
[[1vce]] - PhDPS + SAH<br />
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[[3i4t]] - PhDPS (mutant) – ''Entamoeba histolytica''<br />
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[[3i4t]] - DPS (mutant) – ''Entamoeba histolytica''<br />
== References ==
== References ==
<references/>
<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Current revision

Diphthine synthase complex with S-adenosyl-L-homocysteine (SAH) and Na+ ion 2owu

Drag the structure with the mouse to rotate

3D structures of diphthine synthase

Updated on 15-July-2020

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 - DPS (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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