2dv3: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
← Older edit
No edit summary
No edit summary
 
(13 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:2dv3.jpg|left|200px]]


{{Structure
==Crystal structure of Leu65 to Arg mutant of Diphthine synthase==
|PDB= 2dv3 |SIZE=350|CAPTION= <scene name='initialview01'>2dv3</scene>, resolution 1.90&Aring;
<StructureSection load='2dv3' size='340' side='right'caption='[[2dv3]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene> and <scene name='pdbligand=FMT:FORMIC ACID'>FMT</scene>
<table><tr><td colspan='2'>[[2dv3]] 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=2DV3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2DV3 FirstGlance]. <br>
|ACTIVITY= [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]  
</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>
|GENE= dphB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=53953 Pyrococcus horikoshii])
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <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>
}}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2dv3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dv3 OCA], [https://pdbe.org/2dv3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2dv3 RCSB], [https://www.ebi.ac.uk/pdbsum/2dv3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2dv3 ProSAT], [https://www.topsan.org/Proteins/RSGI/2dv3 TOPSAN]</span></td></tr>
</table>
== 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/dv/2dv3_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=2dv3 ConSurf].
<div style="clear:both"></div>


'''Crystal structure of Leu65 to Arg mutant of Diphthine synthase'''
==See Also==
 
*[[Diphthine synthase|Diphthine synthase]]
 
== References ==
==About this Structure==
<references/>
2DV3 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=2DV3 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: CL]]
[[Category: FMT]]
[[Category: GOL]]
[[Category: NA]]
[[Category: SAH]]
[[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 Thu Mar 20 16:31:56 2008''

Latest revision as of 11:30, 25 October 2023

Crystal structure of Leu65 to Arg mutant of Diphthine synthaseCrystal structure of Leu65 to Arg mutant of Diphthine synthase

Structural highlights

2dv3 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

2dv3, resolution 1.90Å

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=2dv3&oldid=3924140"