This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
2eld
From Proteopedia
(Difference between revisions)
| (2 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
==Mutant L160M structure of PH0725 from Pyrococcus horikoshii OT3== | ==Mutant L160M structure of PH0725 from Pyrococcus horikoshii OT3== | ||
| - | <StructureSection load='2eld' size='340' side='right' caption='[[2eld]], [[Resolution|resolution]] 2.30Å' scene=''> | + | <StructureSection load='2eld' size='340' side='right'caption='[[2eld]], [[Resolution|resolution]] 2.30Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2eld]] is a 2 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[2eld]] 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=2ELD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ELD FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</td></tr> |
| - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <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'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2eld FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2eld OCA], [https://pdbe.org/2eld PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2eld RCSB], [https://www.ebi.ac.uk/pdbsum/2eld PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2eld ProSAT], [https://www.topsan.org/Proteins/RSGI/2eld TOPSAN]</span></td></tr> |
</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]] | ||
| Line 27: | Line 27: | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: Pyrococcus horikoshii | + | [[Category: Pyrococcus horikoshii OT3]] |
| - | + | [[Category: Shimizu K]] | |
| - | [[Category: Shimizu | + | |
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
Current revision
Mutant L160M structure of PH0725 from Pyrococcus horikoshii OT3
| |||||||||||
