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| - | ==TRYPAREDOXIN FROM TRYPANOSOMA BRUCEI== | + | |
| - | <StructureSection load='1o73' size='340' side='right' caption='[[1o73]], [[Resolution|resolution]] 2.28Å' scene=''> | + | ==Tryparedoxin from Trypanosoma brucei== |
| | + | <StructureSection load='1o73' size='340' side='right'caption='[[1o73]], [[Resolution|resolution]] 2.28Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1o73]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Trybb Trybb]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O73 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1O73 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1o73]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Trypanosoma_brucei_brucei Trypanosoma brucei brucei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O73 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1O73 FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1fg4|1fg4]], [[1i5g|1i5g]], [[1o6j|1o6j]], [[1o81|1o81]], [[1oc8|1oc8]], [[1oc9|1oc9]], [[1ewx|1ewx]], [[1ezk|1ezk]], [[1o7u|1o7u]], [[1o85|1o85]], [[1o8w|1o8w]], [[1o8x|1o8x]], [[1qk8|1qk8]]</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]] 2.28Å</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=1o73 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o73 OCA], [http://pdbe.org/1o73 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1o73 RCSB], [http://www.ebi.ac.uk/pdbsum/1o73 PDBsum]</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=1o73 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o73 OCA], [https://pdbe.org/1o73 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1o73 RCSB], [https://www.ebi.ac.uk/pdbsum/1o73 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1o73 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/TYPX_TRYBB TYPX_TRYBB]] Acts as a thiol-disulfide oxidoreductase. It is spontaneously reduced by trypanothione. | + | [https://www.uniprot.org/uniprot/TYPX_TRYBB TYPX_TRYBB] Acts as a thiol-disulfide oxidoreductase. It is spontaneously reduced by trypanothione. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| | Check<jmol> | | Check<jmol> |
| | <jmolCheckbox> | | <jmolCheckbox> |
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/o7/1o73_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/o7/1o73_consurf.spt"</scriptWhenChecked> |
| - | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
| | </jmolCheckbox> | | </jmolCheckbox> |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Trybb]] | + | [[Category: Large Structures]] |
| - | [[Category: Alphey, M S]] | + | [[Category: Trypanosoma brucei brucei]] |
| - | [[Category: Bond, C S]] | + | [[Category: Alphey MS]] |
| - | [[Category: Gabrielsen, M]] | + | [[Category: Bond CS]] |
| - | [[Category: Hunter, W N]] | + | [[Category: Gabrielsen M]] |
| - | [[Category: Electron transport]] | + | [[Category: Hunter WN]] |
| - | [[Category: Thioredoxin]]
| + | |
| - | [[Category: Trypanosoma brucei]]
| + | |
| - | [[Category: Trypanosomatid]]
| + | |
| - | [[Category: Tryparedoxin]]
| + | |
| Structural highlights
Function
TYPX_TRYBB Acts as a thiol-disulfide oxidoreductase. It is spontaneously reduced by trypanothione.
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
Tryparedoxin (TryX) is a member of the thioredoxin (TrX) fold family involved in the regulation of oxidative stress in parasitic trypanosomatids. Like TrX, TryX carries a characteristic Trp-Cys-Xaa-Xaa-Cys motif, which positions a redox-active disulfide underneath a tryptophan lid. We report the structure of a Crithidia fasciculata tryparedoxin isoform (CfTryX2) in two crystal forms and compare them with structures determined previously. Efforts to chemically generate crystals of reduced TryX1 were unsuccessful, and we carried out a novel experiment to break the redox-active disulfide, formed between Cys-40 and Cys-43, utilizing the intense x-radiation from a third generation synchrotron undulator beamline. A time course study of the S-S bond cleavage is reported with the structure of a TryX1 C43A mutant as the control. When freed from the constraints of a disulfide link to Cys-43, Cys-40 pivots to become slightly more solvent-accessible. In addition, we have determined the structure of Trypanosoma brucei TryX, which, influenced by the molecular packing in the crystal lattice, displays a significantly different orientation of the active site tryptophan lid. This structural change may be of functional significance when TryX interacts with tryparedoxin peroxidase, the final protein in the trypanothione-dependent peroxidase pathway. Comparisons with chloroplast TrX and its substrate fructose 1,6-bisphosphate phosphatase suggest that this movement may represent a general feature of redox regulation in the trypanothione and thioredoxin peroxidase pathways.
Tryparedoxins from Crithidia fasciculata and Trypanosoma brucei: photoreduction of the redox disulfide using synchrotron radiation and evidence for a conformational switch implicated in function.,Alphey MS, Gabrielsen M, Micossi E, Leonard GA, McSweeney SM, Ravelli RB, Tetaud E, Fairlamb AH, Bond CS, Hunter WN J Biol Chem. 2003 Jul 11;278(28):25919-25. Epub 2003 Apr 21. PMID:12707277[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Alphey MS, Gabrielsen M, Micossi E, Leonard GA, McSweeney SM, Ravelli RB, Tetaud E, Fairlamb AH, Bond CS, Hunter WN. Tryparedoxins from Crithidia fasciculata and Trypanosoma brucei: photoreduction of the redox disulfide using synchrotron radiation and evidence for a conformational switch implicated in function. J Biol Chem. 2003 Jul 11;278(28):25919-25. Epub 2003 Apr 21. PMID:12707277 doi:10.1074/jbc.M301526200
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