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[[Image:2ek3.jpg|left|200px]]<br /><applet load="2ek3" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2ek3, resolution 2.80&Aring;" />
'''Structural study of Project ID PH0725 from Pyrococcus horikoshii OT3 (L3M)'''<br />


==About this Structure==
==Structural study of Project ID PH0725 from Pyrococcus horikoshii OT3 (L3M)==
2EK3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pyrococcus_horikoshii Pyrococcus horikoshii] with <scene name='pdbligand=NA:'>NA</scene> and <scene name='pdbligand=SAH:'>SAH</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Diphthine_synthase Diphthine synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.98 2.1.1.98] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EK3 OCA].
<StructureSection load='2ek3' size='340' side='right'caption='[[2ek3]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
[[Category: Diphthine synthase]]
== Structural highlights ==
[[Category: Pyrococcus horikoshii]]
<table><tr><td colspan='2'>[[2ek3]] 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=2EK3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2EK3 FirstGlance]. <br>
[[Category: Single protein]]
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</td></tr>
[[Category: Asada, Y.]]
<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>
[[Category: Kunishima, N.]]
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ek3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ek3 OCA], [https://pdbe.org/2ek3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ek3 RCSB], [https://www.ebi.ac.uk/pdbsum/2ek3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ek3 ProSAT], [https://www.topsan.org/Proteins/RSGI/2ek3 TOPSAN]</span></td></tr>
[[Category: Matsuura, Y.]]
</table>
[[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]]
== Function ==
[[Category: Shimada, H.]]
[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>
[[Category: Taketa, M.]]
== Evolutionary Conservation ==
[[Category: NA]]
[[Image:Consurf_key_small.gif|200px|right]]
[[Category: SAH]]
Check<jmol>
[[Category: national project on protein structural and functional analyses]]
  <jmolCheckbox>
[[Category: nppsfa]]
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ek/2ek3_consurf.spt"</scriptWhenChecked>
[[Category: riken structural genomics/proteomics initiative]]
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
[[Category: rsgi]]
    <text>to colour the structure by Evolutionary Conservation</text>
[[Category: structural genomics]]
  </jmolCheckbox>
[[Category: transferase]]
</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=2ek3 ConSurf].
<div style="clear:both"></div>


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:11:51 2008''
==See Also==
*[[Diphthine synthase|Diphthine synthase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pyrococcus horikoshii OT3]]
[[Category: Asada Y]]
[[Category: Kunishima N]]
[[Category: Matsuura Y]]
[[Category: Shimada H]]
[[Category: Taketa M]]

Latest revision as of 21:51, 29 May 2024

Structural study of Project ID PH0725 from Pyrococcus horikoshii OT3 (L3M)Structural study of Project ID PH0725 from Pyrococcus horikoshii OT3 (L3M)

Structural highlights

2ek3 is a 2 chain structure with sequence from Pyrococcus horikoshii OT3. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.8Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN

Function

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.[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

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

2ek3, resolution 2.80Å

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