3dh9: Difference between revisions

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'''Unreleased structure'''


The entry 3dh9 is ON HOLD  until Paper Publication
==Crystal Structure of Drosophila Thioredoxin Reductase, wild-type==
<StructureSection load='3dh9' size='340' side='right'caption='[[3dh9]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
== Structural highlights ==
<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>
</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>
<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>
<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>


Authors: Eckenroth, B.E., Hondal, R.J., Everse, SJ.
==See Also==
 
*[[Thioredoxin reductase 3D structures|Thioredoxin reductase 3D structures]]
Description: Crystal Structure of Drosophila Thioredoxin Reductase, wild-type
== References ==
 
<references/>
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Dec 24 11:26:56 2008''
__TOC__
</StructureSection>
[[Category: Drosophila melanogaster]]
[[Category: Large Structures]]
[[Category: Eckenroth BE]]
[[Category: Everse SJ]]
[[Category: Hondal RJ]]

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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