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| | <StructureSection load='6zmu' size='340' side='right'caption='[[6zmu]], [[Resolution|resolution]] 1.95Å' scene=''> | | <StructureSection load='6zmu' size='340' side='right'caption='[[6zmu]], [[Resolution|resolution]] 1.95Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6zmu]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Drome Drome]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ZMU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6ZMU FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6zmu]] is a 4 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=6ZMU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6ZMU FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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]] 1.95Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[6z7o|6z7o]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">dhd, Trx-1, CG4193 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 DROME])</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=6zmu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6zmu OCA], [https://pdbe.org/6zmu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6zmu RCSB], [https://www.ebi.ac.uk/pdbsum/6zmu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6zmu ProSAT]</span></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=6zmu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6zmu OCA], [https://pdbe.org/6zmu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6zmu RCSB], [https://www.ebi.ac.uk/pdbsum/6zmu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6zmu ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/THIO1_DROME THIO1_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. Required for female meiosis and early embryonic development.<ref>PMID:11877442</ref> <ref>PMID:9106167</ref>
| + | [https://www.uniprot.org/uniprot/THIO1_DROME THIO1_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. Required for female meiosis and early embryonic development.<ref>PMID:11877442</ref> <ref>PMID:9106167</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 6zmu" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6zmu" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Thioredoxin 3D structures|Thioredoxin 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Drome]] | + | [[Category: Drosophila melanogaster]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Baginski, B]] | + | [[Category: Baginski B]] |
| - | [[Category: Macias, M J]] | + | [[Category: Macias MJ]] |
| - | [[Category: Pluta, R]] | + | [[Category: Pluta R]] |
| - | [[Category: Dna-binding]]
| + | |
| - | [[Category: Homeostasis]]
| + | |
| - | [[Category: Oocyte-to-embryo]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Protamine]]
| + | |
| - | [[Category: Redox]]
| + | |
| - | [[Category: Sperm]]
| + | |
| Structural highlights
Function
THIO1_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. Required for female meiosis and early embryonic development.[1] [2]
Publication Abstract from PubMed
Thioredoxins (Trxs) are ubiquitous enzymes that regulate the redox state in cells. In Drosophila, there are two germline-specific Trxs, Deadhead (Dhd) and thioredoxin T (TrxT), that belong to the lethal(3)malignant brain tumor signature genes and to the 'survival network' of genes that mediate the cellular response to DNA damage. Dhd is a maternal protein required for early embryogenesis that promotes protamine-histone exchange in fertilized eggs and midblastula transition. TrxT is testis-specific and associates with the lampbrush loops of the Y chromosome. Here, the first structures of Dhd and TrxT are presented, unveiling new features of these two thioredoxins. Dhd has positively charged patches on its surface, in contrast to the negatively charged surfaces commonly found in most Trxs. This distinctive charge distribution helps to define initial encounter complexes with DNA/RNA that will lead to final specific interactions with cofactors to promote chromatin remodeling. TrxT contains a C-terminal extension, which is mostly unstructured and highly flexible, that wraps the conserved core through a closed conformation. It is believed that these new structures can guide future work aimed at understanding embryo development and redox homeostasis in Drosophila. Moreover, due to their restricted presence in Schizophora (a section of the true flies), these structures can help in the design of small-molecular binders to modulate native redox homeostasis, thereby providing new applications for the control of plagues that cause human diseases and/or bring about economic losses by damaging crop production.
Structures of the germline-specific Deadhead and thioredoxin T proteins from Drosophila melanogaster reveal unique features among thioredoxins.,Freier R, Aragon E, Baginski B, Pluta R, Martin-Malpartida P, Ruiz L, Condeminas M, Gonzalez C, Macias MJ IUCrJ. 2021 Feb 11;8(Pt 2):281-294. doi: 10.1107/S2052252521000221. eCollection, 2021 Mar 1. PMID:33708404[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
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
- ↑ Pellicena-Palle A, Stitzinger SM, Salz HK. The function of the Drosophila thioredoxin homologue encoded by the deadhead gene is redox-dependent and blocks the initiation of development but not DNA synthesis. Mech Dev. 1997 Feb;62(1):61-5. doi: 10.1016/s0925-4773(96)00650-8. PMID:9106167 doi:http://dx.doi.org/10.1016/s0925-4773(96)00650-8
- ↑ Freier R, Aragon E, Baginski B, Pluta R, Martin-Malpartida P, Ruiz L, Condeminas M, Gonzalez C, Macias MJ. Structures of the germline-specific Deadhead and thioredoxin T proteins from Drosophila melanogaster reveal unique features among thioredoxins. IUCrJ. 2021 Feb 11;8(Pt 2):281-294. doi: 10.1107/S2052252521000221. eCollection, 2021 Mar 1. PMID:33708404 doi:http://dx.doi.org/10.1107/S2052252521000221
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