2owf: Difference between revisions

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New page: left|200px<br /><applet load="2owf" size="450" color="white" frame="true" align="right" spinBox="true" caption="2owf, resolution 2.20Å" /> '''Crystal structure of...
 
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[[Image:2owf.jpg|left|200px]]<br /><applet load="2owf" size="450" color="white" frame="true" align="right" spinBox="true"
caption="2owf, resolution 2.20&Aring;" />
'''Crystal structure of PH0725 from Pyrococcus horikoshii OT3'''<br />


==About this Structure==
==Crystal structure of PH0725 from Pyrococcus horikoshii OT3==
2OWF 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 SAH as [http://en.wikipedia.org/wiki/ligand ligand]. 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=2OWF OCA].
<StructureSection load='2owf' size='340' side='right'caption='[[2owf]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
[[Category: Diphthine synthase]]
== Structural highlights ==
[[Category: Pyrococcus horikoshii]]
<table><tr><td colspan='2'>[[2owf]] is a 1 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=2OWF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2OWF 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]] 2.2&#8491;</td></tr>
[[Category: Kunishima, N.]]
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr>
[[Category: Matsuura, Y.]]
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2owf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2owf OCA], [https://pdbe.org/2owf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2owf RCSB], [https://www.ebi.ac.uk/pdbsum/2owf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2owf ProSAT], [https://www.topsan.org/Proteins/RSGI/2owf TOPSAN]</span></td></tr>
[[Category: Morikawa, 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: Sugahara, M.]]
== Evolutionary Conservation ==
[[Category: SAH]]
[[Image:Consurf_key_small.gif|200px|right]]
[[Category: national project on protein structural and functional analyses]]
Check<jmol>
[[Category: nppsfa]]
  <jmolCheckbox>
[[Category: pyrococcus horikoshii ot3]]
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ow/2owf_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=2owf ConSurf].
<div style="clear:both"></div>


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 13:20:12 2007''
==See Also==
*[[Diphthine synthase|Diphthine synthase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pyrococcus horikoshii OT3]]
[[Category: Kunishima N]]
[[Category: Matsuura Y]]
[[Category: Morikawa Y]]
[[Category: Shimada H]]
[[Category: Sugahara M]]

Latest revision as of 11:58, 25 October 2023

Crystal structure of PH0725 from Pyrococcus horikoshii OT3Crystal structure of PH0725 from Pyrococcus horikoshii OT3

Structural highlights

2owf is a 1 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 2.2Å
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

2owf, resolution 2.20Å

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