1o85: Difference between revisions
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==Radiation-reduced Tryparedoxin-I== | |||
<StructureSection load='1o85' size='340' side='right' caption='[[1o85]], [[Resolution|resolution]] 1.50Å' scene=''> | <StructureSection load='1o85' size='340' side='right' caption='[[1o85]], [[Resolution|resolution]] 1.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1o85]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Crifa Crifa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O85 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1O85 FirstGlance]. <br> | <table><tr><td colspan='2'>[[1o85]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Crifa Crifa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O85 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1O85 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]], [[1o73|1o73]], [[1o81|1o81]], [[1oc8|1oc8]], [[1oc9|1oc9]], [[1ewx|1ewx]], [[1ezk|1ezk]], [[1o7u|1o7u]], [[1o8w|1o8w]], [[1o8x|1o8x]], [[1qk8|1qk8]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1fg4|1fg4]], [[1i5g|1i5g]], [[1o6j|1o6j]], [[1o73|1o73]], [[1o81|1o81]], [[1oc8|1oc8]], [[1oc9|1oc9]], [[1ewx|1ewx]], [[1ezk|1ezk]], [[1o7u|1o7u]], [[1o8w|1o8w]], [[1o8x|1o8x]], [[1qk8|1qk8]]</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=1o85 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o85 OCA], [http://pdbe.org/1o85 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1o85 RCSB], [http://www.ebi.ac.uk/pdbsum/1o85 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=1o85 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o85 OCA], [http://pdbe.org/1o85 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1o85 RCSB], [http://www.ebi.ac.uk/pdbsum/1o85 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1o85 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
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Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/o8/1o85_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/o8/1o85_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
Revision as of 10:36, 7 February 2018
Radiation-reduced Tryparedoxin-IRadiation-reduced Tryparedoxin-I
Structural highlights
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 PubMedTryparedoxin (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
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