2ed5: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
New page: left|200px<br /><applet load="2ed5" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ed5, resolution 2.10Å" /> '''Mutant S147M structu...
 
No edit summary
 
(16 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:2ed5.jpg|left|200px]]<br /><applet load="2ed5" size="450" color="white" frame="true" align="right" spinBox="true"
caption="2ed5, resolution 2.10&Aring;" />
'''Mutant S147M structure of PH0725 from Pyrococcus horikoshii OT3'''<br />


==About this Structure==
==Mutant S147M structure of PH0725 from Pyrococcus horikoshii OT3==
2ED5 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 NA, SAH and GOL 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=2ED5 OCA].
<StructureSection load='2ed5' size='340' side='right'caption='[[2ed5]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
[[Category: Diphthine synthase]]
== Structural highlights ==
[[Category: Pyrococcus horikoshii]]
<table><tr><td colspan='2'>[[2ed5]] 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=2ED5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ED5 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]] 2.1&#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=2ed5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ed5 OCA], [https://pdbe.org/2ed5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ed5 RCSB], [https://www.ebi.ac.uk/pdbsum/2ed5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ed5 ProSAT], [https://www.topsan.org/Proteins/RSGI/2ed5 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/ed/2ed5_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=2ed5 ConSurf].
<div style="clear:both"></div>


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 10:01:01 2007''
==See Also==
*[[Diphthine synthase|Diphthine synthase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pyrococcus horikoshii OT3]]
[[Category: Shimizu K]]

Latest revision as of 11:38, 25 October 2023

Mutant S147M structure of PH0725 from Pyrococcus horikoshii OT3Mutant S147M structure of PH0725 from Pyrococcus horikoshii OT3

Structural highlights

2ed5 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 2.1Å
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

2ed5, resolution 2.10Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA
Retrieved from "https://proteopedia.openfox.io/wiki/index.php?title=2ed5&oldid=3924576"