3dh9: Difference between revisions

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[[Image:3dh9.jpg|left|200px]]


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==Crystal Structure of Drosophila Thioredoxin Reductase, wild-type==
The line below this paragraph, containing "STRUCTURE_3dh9", creates the "Structure Box" on the page.
<StructureSection load='3dh9' size='340' side='right'caption='[[3dh9]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[3dh9]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3DH9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3DH9 FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.25&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr>
{{STRUCTURE_3dh9| PDB=3dh9 |  SCENE= }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3dh9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3dh9 OCA], [https://pdbe.org/3dh9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3dh9 RCSB], [https://www.ebi.ac.uk/pdbsum/3dh9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3dh9 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/TRXR1_DROME TRXR1_DROME] Thioredoxin system is a major player in glutathione metabolism, due to the demonstrated absence of a glutathione reductase. Functionally interacts with the Sod/Cat reactive oxidation species (ROS) defense system and thereby has a role in preadult development and life span. Lack of a glutathione reductase suggests antioxidant defense in Drosophila, and probably in related insects, differs fundamentally from that in other organisms.<ref>PMID:11158675</ref> <ref>PMID:11525742</ref> <ref>PMID:11796729</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/dh/3dh9_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=3dh9 ConSurf].
<div style="clear:both"></div>


===Crystal Structure of Drosophila Thioredoxin Reductase, wild-type===
==See Also==
 
*[[Thioredoxin reductase 3D structures|Thioredoxin reductase 3D structures]]
 
== References ==
==About this Structure==
<references/>
3DH9 is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3DH9 OCA].
__TOC__
</StructureSection>
[[Category: Drosophila melanogaster]]
[[Category: Drosophila melanogaster]]
[[Category: Thioredoxin-disulfide reductase]]
[[Category: Large Structures]]
[[Category: Eckenroth, B E.]]
[[Category: Eckenroth BE]]
[[Category: Everse, SJ.]]
[[Category: Everse SJ]]
[[Category: Hondal, R J.]]
[[Category: Hondal RJ]]
[[Category: Alternative initiation]]
[[Category: Alternative splicing]]
[[Category: Cytoplasm]]
[[Category: Fad]]
[[Category: Flavoprotein]]
[[Category: Mitochondrion]]
[[Category: Nadp]]
[[Category: Oxidoreductase]]
[[Category: Redox-active center]]
[[Category: Rossmann]]
[[Category: Transit peptide]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun 17 11:22:12 2009''

Latest revision as of 11:59, 30 October 2024

Crystal Structure of Drosophila Thioredoxin Reductase, wild-typeCrystal Structure of Drosophila Thioredoxin Reductase, wild-type

Structural highlights

3dh9 is a 2 chain structure with sequence from Drosophila melanogaster. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.25Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

TRXR1_DROME Thioredoxin system is a major player in glutathione metabolism, due to the demonstrated absence of a glutathione reductase. Functionally interacts with the Sod/Cat reactive oxidation species (ROS) defense system and thereby has a role in preadult development and life span. Lack of a glutathione reductase suggests antioxidant defense in Drosophila, and probably in related insects, differs fundamentally from that in other organisms.[1] [2] [3]

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. ↑ Kanzok SM, Fechner A, Bauer H, Ulschmid JK, Muller HM, Botella-Munoz J, Schneuwly S, Schirmer R, Becker K. Substitution of the thioredoxin system for glutathione reductase in Drosophila melanogaster. Science. 2001 Jan 26;291(5504):643-6. PMID:11158675 doi:http://dx.doi.org/10.1126/science.291.5504.643
  2. ↑ Missirlis F, Phillips JP, Jackle H. Cooperative action of antioxidant defense systems in Drosophila. Curr Biol. 2001 Aug 21;11(16):1272-7. PMID:11525742
  3. ↑ Missirlis F, Ulschmid JK, Hirosawa-Takamori M, Gronke S, Schafer U, Becker K, Phillips JP, Jackle H. Mitochondrial and cytoplasmic thioredoxin reductase variants encoded by a single Drosophila gene are both essential for viability. J Biol Chem. 2002 Mar 29;277(13):11521-6. Epub 2002 Jan 16. PMID:11796729 doi:http://dx.doi.org/10.1074/jbc.M111692200

3dh9, resolution 2.25Å

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