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[[Image:2ehc.jpg|left|200px]]


{{Structure
==Crystal structure of Asn69 to Lys mutant of Diphthine synthase==
|PDB= 2ehc |SIZE=350|CAPTION= <scene name='initialview01'>2ehc</scene>, resolution 1.80&Aring;
<StructureSection load='2ehc' size='340' side='right'caption='[[2ehc]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
<table><tr><td colspan='2'>[[2ehc]] 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=2EHC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2EHC FirstGlance]. <br>
|ACTIVITY= <span class='plainlinks'>[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] </span>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
|GENE=
<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=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
|DOMAIN=
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ehc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ehc OCA], [https://pdbe.org/2ehc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ehc RCSB], [https://www.ebi.ac.uk/pdbsum/2ehc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ehc ProSAT], [https://www.topsan.org/Proteins/RSGI/2ehc TOPSAN]</span></td></tr>
|RELATEDENTRY=[[1wng|1WNG]]
</table>
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ehc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ehc OCA], [http://www.ebi.ac.uk/pdbsum/2ehc PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2ehc RCSB]</span>
== 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/eh/2ehc_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=2ehc ConSurf].
<div style="clear:both"></div>


'''Crystal structure of Asn69 to Lys mutant of Diphthine synthase'''
==See Also==
 
*[[Diphthine synthase|Diphthine synthase]]
 
== References ==
==About this Structure==
<references/>
2EHC is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pyrococcus_horikoshii Pyrococcus horikoshii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EHC OCA].
__TOC__
[[Category: Diphthine synthase]]
</StructureSection>
[[Category: Pyrococcus horikoshii]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Pyrococcus horikoshii OT3]]
[[Category: Kunishima, N.]]
[[Category: Kunishima N]]
[[Category: Matsuura, Y.]]
[[Category: Matsuura Y]]
[[Category: Mizutani, H.]]
[[Category: Mizutani H]]
[[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]]
[[Category: national project on protein structural and functional analyse]]
[[Category: nppsfa]]
[[Category: riken structural genomics/proteomics initiative]]
[[Category: rsgi]]
[[Category: structural genomic]]
[[Category: transferase]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:49:05 2008''

Latest revision as of 11:40, 25 October 2023

Crystal structure of Asn69 to Lys mutant of Diphthine synthaseCrystal structure of Asn69 to Lys mutant of Diphthine synthase

Structural highlights

2ehc 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 1.8Å
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

2ehc, resolution 1.80Å

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