Diphthine synthase: Difference between revisions
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<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. | '''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/5'>SAH binding site</scene>. | |||
<scene name='52/525183/Cv/6'>Na coordination site</scene> ([[2owu]]), water molecules shown as red spheres. | |||
</StructureSection> | |||
==3D structures of diphthine synthase== | ==3D structures of diphthine synthase== | ||
Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}} | |||
[[1vhv]] – DPS – ''Archaeoglobus fulgidus''<br /> | [[1vhv]] – DPS – ''Archaeoglobus fulgidus''<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]] – | [[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 /> | |||
[[3i4t]] - DPS (mutant) – ''Entamoeba histolytica''<br /> | |||
== References == | |||
<references/> | |||
[[Category:Topic Page]] | |||
Latest revision as of 13:07, 15 July 2020
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] . (2owu), water molecules shown as red spheres. |
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3D structures of diphthine synthase3D 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
ReferencesReferences
- ↑ 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