3dh9: Difference between revisions

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<StructureSection load='3dh9' size='340' side='right' caption='[[3dh9]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
<StructureSection load='3dh9' size='340' side='right' caption='[[3dh9]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3dh9]] is a 2 chain structure with sequence 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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3DH9 FirstGlance]. <br>
<table><tr><td colspan='2'>[[3dh9]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Drome Drome]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3DH9 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2nvk|2nvk]], [[3dgh|3dgh]]</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2nvk|2nvk]], [[3dgh|3dgh]]</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Trxr-1, GR, CG2151 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 Drosophila melanogaster])</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Trxr-1, GR, CG2151 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 DROME])</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Thioredoxin-disulfide_reductase Thioredoxin-disulfide reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.1.9 1.8.1.9] </span></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Thioredoxin-disulfide_reductase Thioredoxin-disulfide reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.1.9 1.8.1.9] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3dh9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3dh9 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3dh9 RCSB], [http://www.ebi.ac.uk/pdbsum/3dh9 PDBsum]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3dh9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3dh9 OCA], [http://pdbe.org/3dh9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3dh9 RCSB], [http://www.ebi.ac.uk/pdbsum/3dh9 PDBsum]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </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/chain_selection.php?pdb_ID=2ata ConSurf].
</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>
<div style="clear:both"></div>


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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Drosophila melanogaster]]
[[Category: Drome]]
[[Category: Thioredoxin-disulfide reductase]]
[[Category: Thioredoxin-disulfide reductase]]
[[Category: Eckenroth, B E]]
[[Category: Eckenroth, B E]]

Revision as of 03:24, 8 February 2016

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 Drome. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Gene:Trxr-1, GR, CG2151 (DROME)
Activity:Thioredoxin-disulfide reductase, with EC number 1.8.1.9
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum

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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