1o85: Difference between revisions

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-{{STRUCTURE_1o85|  PDB=1o85  |  SCENE=  }}
-===RADIATION-REDUCED TRYPAREDOXIN-I===
-{{ABSTRACT_PUBMED_12707277}}
-==About this Structure==
+==Radiation-reduced Tryparedoxin-I==
-[[1o85]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Crithidia_fasciculata Crithidia fasciculata]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O85 OCA].
+<StructureSection load='1o85' size='340' side='right'caption='[[1o85]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1o85]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Crithidia_fasciculata Crithidia fasciculata]. 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 [https://proteopedia.org/fgij/fg.htm?mol=1O85 FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5&#8491;</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=1o85 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o85 OCA], [https://pdbe.org/1o85 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1o85 RCSB], [https://www.ebi.ac.uk/pdbsum/1o85 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1o85 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/O96438_CRIFA O96438_CRIFA]
+== 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/o8/1o85_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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/main_output.php?pdb_ID=1o85 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== 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.
-==Reference==
+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<ref>PMID:12707277</ref>
-<ref group="xtra">PMID:012707277</ref><references group="xtra"/><references/>
-[[Category: Crithidia fasciculata]]
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Alphey, M S.]]
+</div>
-[[Category: Bond, C S.]]
+<div class="pdbe-citations 1o85" style="background-color:#fffaf0;"></div>
-[[Category: Hunter, W N.]]
+== References ==
-[[Category: Anomalous dispersion]]
+<references/>
+__TOC__
+</StructureSection>
 [[Category: Crithidia fasciculata]]
-[[Category: Disulfide bonds tryparedoxin]]
+[[Category: Large Structures]]
-[[Category: Electron transport]]
+[[Category: Alphey MS]]
-[[Category: Oxidative stress]]
+[[Category: Bond CS]]
-[[Category: Oxidoreductase]]
+[[Category: Hunter WN]]
-[[Category: Synchrotron radiation]]
-[[Category: Thioredoxin]]
-[[Category: Trypanosome]]
-[[Category: Tryparedoxin-i]]