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1xwc

From Proteopedia

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Drosophila thioredoxin, reduced, P6522

Structural highlights

1xwc is a 1 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 2.3Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

THIO2_DROME Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions. As a reducing substrate of peroxiredoxin 1, thioredoxin 2 is preferred over thioredoxin 1.^[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Thioredoxins (Trx) participate in essential antioxidant and redox-regulatory processes via a pair of conserved cysteine residues. In dipteran insects like Drosophila and Anopheles, which lack a genuine glutathione reductase (GR), thioredoxins fuel the glutathione system with reducing equivalents. Thus, characterizing Trxs from these organisms contributes to our understanding of redox control in GR-free systems and provides information on novel targets for insect control. Cytosolic Trx of Drosophila melanogaster (DmTrx) is the first thioredoxin that was crystallized for X-ray diffraction analysis in the reduced and in the oxidized form. Comparison of the resulting structures shows rearrangements in the active-site regions. Formation of the C32-C35 disulfide bridge leads to a rotation of the side-chain of C32 away from C35 in the reduced form. This is similar to the situation in human Trx and Trx m from spinach chloroplasts but differs from Escherichia coli Trx, where it is C35 that moves upon change of the redox state. In all four crystal forms that were analysed, DmTrx molecules are engaged in a non-covalent dimer interaction. However, as demonstrated by gel-filtration analyses, DmTrx does not dimerize under quasi in vivo conditions and there is no redox control of a putative monomer/dimer equilibrium. The dimer dissociation constants K(d) were found to be 2.2mM for reduced DmTrx and above 10mM for oxidized DmTrx as well as for the protein in the presence of reduced glutathione. In human Trx, oxidative dimerization has been demonstrated in vitro. Therefore, this finding may indicate a difference in redox control of GR-free and GR-containing organisms.

Comparative structural analysis of oxidized and reduced thioredoxin from Drosophila melanogaster.,Wahl MC, Irmler A, Hecker B, Schirmer RH, Becker K J Mol Biol. 2005 Feb 4;345(5):1119-30. Epub 2004 Dec 16. PMID:15644209^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Bauer H, Kanzok SM, Schirmer RH. Thioredoxin-2 but not thioredoxin-1 is a substrate of thioredoxin peroxidase-1 from Drosophila melanogaster: isolation and characterization of a second thioredoxin in D. Melanogaster and evidence for distinct biological functions of Trx-1 and Trx-2. J Biol Chem. 2002 May 17;277(20):17457-63. Epub 2002 Mar 4. PMID:11877442 doi:http://dx.doi.org/10.1074/jbc.M200636200
↑ Wahl MC, Irmler A, Hecker B, Schirmer RH, Becker K. Comparative structural analysis of oxidized and reduced thioredoxin from Drosophila melanogaster. J Mol Biol. 2005 Feb 4;345(5):1119-30. Epub 2004 Dec 16. PMID:15644209 doi:10.1016/j.jmb.2004.11.004

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1xwc"

@@ Line 1: / Line 1: @@
 ==Drosophila thioredoxin, reduced, P6522==
-<StructureSection load='1xwc' size='340' side='right' caption='[[1xwc]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
+<StructureSection load='1xwc' size='340' side='right'caption='[[1xwc]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1xwc]] is a 1 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=1XWC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1XWC FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1xwc]] is a 1 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=1XWC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XWC FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1xw9|1xw9]], [[1xwa|1xwa]], [[1xwb|1xwb]]</td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TRX-2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 Drosophila melanogaster])</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=1xwc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xwc OCA], [https://pdbe.org/1xwc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xwc RCSB], [https://www.ebi.ac.uk/pdbsum/1xwc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xwc ProSAT]</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=1xwc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xwc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1xwc RCSB], [http://www.ebi.ac.uk/pdbsum/1xwc PDBsum]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/THIO2_DROME THIO2_DROME]] Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions. As a reducing substrate of peroxiredoxin 1, thioredoxin 2 is preferred over thioredoxin 1.<ref>PMID:11877442</ref>
+[https://www.uniprot.org/uniprot/THIO2_DROME THIO2_DROME] Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions. As a reducing substrate of peroxiredoxin 1, thioredoxin 2 is preferred over thioredoxin 1.<ref>PMID:11877442</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/xw/1xwc_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/xw/1xwc_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/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=1xwc ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ Line 27: / Line 27: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 1xwc" style="background-color:#fffaf0;"></div>
 ==See Also==
-*[[Thioredoxin|Thioredoxin]]
+*[[Thioredoxin 3D structures|Thioredoxin 3D structures]]
 == References ==
 <references/>
@@ Line 35: / Line 36: @@
 </StructureSection>
 [[Category: Drosophila melanogaster]]
-[[Category: Becker, K]]
+[[Category: Large Structures]]
-[[Category: Hecker, B]]
+[[Category: Becker K]]
-[[Category: Irmler, A]]
+[[Category: Hecker B]]
-[[Category: Schirmer, R H]]
+[[Category: Irmler A]]
-[[Category: Wahl, M C]]
+[[Category: Schirmer RH]]
-[[Category: Dimerization]]
+[[Category: Wahl MC]]
-[[Category: Electron transport]]
-[[Category: Redox regulation]]
-[[Category: Thioredoxin]]
-[[Category: X-ray crystal structure]]

1xwc

From Proteopedia

Current revision

Drosophila thioredoxin, reduced, P6522

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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