2en5: Difference between revisions

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[[Image:2en5.jpg|left|200px]]<br /><applet load="2en5" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2en5, resolution 1.90&Aring;" />
'''Mutant R262H structure of PH0725 from Pyrococcus horikoshii OT3'''<br />


==About this Structure==
==Mutant R262H structure of PH0725 from Pyrococcus horikoshii OT3==
2EN5 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>, <scene name='pdbligand=SAH:'>SAH</scene> and <scene name='pdbligand=GOL:'>GOL</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=2EN5 OCA].
<StructureSection load='2en5' size='340' side='right'caption='[[2en5]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
[[Category: Diphthine synthase]]
== Structural highlights ==
[[Category: Pyrococcus horikoshii]]
<table><tr><td colspan='2'>[[2en5]] 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=2EN5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2EN5 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]] 1.9&#8491;</td></tr>
[[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]]
<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>
[[Category: Shimizu, K.]]
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2en5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2en5 OCA], [https://pdbe.org/2en5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2en5 RCSB], [https://www.ebi.ac.uk/pdbsum/2en5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2en5 ProSAT], [https://www.topsan.org/Proteins/RSGI/2en5 TOPSAN]</span></td></tr>
[[Category: GOL]]
</table>
[[Category: NA]]
== Function ==
[[Category: SAH]]
[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: national project on protein structural and functional analyses]]
== Evolutionary Conservation ==
[[Category: nppsfa]]
[[Image:Consurf_key_small.gif|200px|right]]
[[Category: riken structural genomics/proteomics initiative]]
Check<jmol>
[[Category: rsgi]]
  <jmolCheckbox>
[[Category: structural genomics]]
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/en/2en5_consurf.spt"</scriptWhenChecked>
[[Category: transferase]]
    <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=2en5 ConSurf].
<div style="clear:both"></div>


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:12:51 2008''
==See Also==
*[[Diphthine synthase|Diphthine synthase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pyrococcus horikoshii OT3]]
[[Category: Shimizu K]]

Latest revision as of 11:42, 25 October 2023

Mutant R262H structure of PH0725 from Pyrococcus horikoshii OT3Mutant R262H structure of PH0725 from Pyrococcus horikoshii OT3

Structural highlights

2en5 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 1.9Å
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

2en5, resolution 1.90Å

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