2e8r: Difference between revisions
Jump to navigation
Jump to search
No edit summary |
No edit summary |
||
(12 intermediate revisions by the same user not shown) | |||
Line 1: | Line 1: | ||
==Structural study of Project ID PH0725 from Pyrococcus horikoshii OT3== | |||
<StructureSection load='2e8r' size='340' side='right'caption='[[2e8r]], [[Resolution|resolution]] 2.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2e8r]] 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=2E8R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2E8R FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> | |||
<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=2e8r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2e8r OCA], [https://pdbe.org/2e8r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2e8r RCSB], [https://www.ebi.ac.uk/pdbsum/2e8r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2e8r ProSAT], [https://www.topsan.org/Proteins/RSGI/2e8r TOPSAN]</span></td></tr> | |||
</table> | |||
== 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 == | |||
== | [[Image:Consurf_key_small.gif|200px|right]] | ||
Check<jmol> | |||
[[ | <jmolCheckbox> | ||
[[ | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/e8/2e8r_consurf.spt"</scriptWhenChecked> | ||
[[ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
[[ | <text>to colour the structure by Evolutionary Conservation</text> | ||
[[ | </jmolCheckbox> | ||
[[ | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2e8r ConSurf]. | ||
[ | <div style="clear:both"></div> | ||
[ | == References == | ||
[[Category: | <references/> | ||
[[Category: | __TOC__ | ||
[[Category: | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Pyrococcus horikoshii OT3]] | ||
[[Category: | [[Category: Asada Y]] | ||
[[Category: | [[Category: Kunishima N]] | ||
[[Category: Matsuura Y]] | |||
[[Category: Shimada H]] | |||
[[Category: Taketa M]] |
Latest revision as of 21:48, 29 May 2024
Structural study of Project ID PH0725 from Pyrococcus horikoshii OT3Structural study of Project ID PH0725 from Pyrococcus horikoshii OT3
Structural highlights
FunctionDPHB_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.[1] Evolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. References
|
|