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2e8s
From Proteopedia
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<StructureSection load='2e8s' size='340' side='right'caption='[[2e8s]], [[Resolution|resolution]] 2.50Å' scene=''> | <StructureSection load='2e8s' size='340' side='right'caption='[[2e8s]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2e8s]] is a 2 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[2e8s]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_horikoshii_OT3 Pyrococcus horikoshii OT3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2E8S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2E8S FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5Å</td></tr> |
| - | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr> |
| - | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2e8s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2e8s OCA], [https://pdbe.org/2e8s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2e8s RCSB], [https://www.ebi.ac.uk/pdbsum/2e8s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2e8s ProSAT], [https://www.topsan.org/Proteins/RSGI/2e8s TOPSAN]</span></td></tr> | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [ | + | [https://www.uniprot.org/uniprot/DPHB_PYRHO DPHB_PYRHO] S-adenosyl-L-methionine-dependent methyltransferase that catalyzes the trimethylation of the amino group of the modified target histidine residue in translation elongation factor 2 (EF-2), to form an intermediate called diphthine. The three successive methylation reactions represent the second step of diphthamide biosynthesis.<ref>PMID:20873788</ref> |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: Diphthine synthase]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Pyrococcus horikoshii]] | + | [[Category: Pyrococcus horikoshii OT3]] |
| - | [[Category: Asada | + | [[Category: Asada Y]] |
| - | [[Category: Kunishima | + | [[Category: Kunishima N]] |
| - | [[Category: Nakamoto | + | [[Category: Nakamoto T]] |
| - | + | [[Category: Shimada H]] | |
| - | [[Category: Shimada | + | [[Category: Taketa M]] |
| - | [[Category: Taketa | + | |
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Current revision
Structural study of Project ID PH0725 from Pyrococcus horikoshii OT3
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