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1o8x

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Mutant tryparedoxin-I Cys43Ala

Structural highlights

1o8x is a 1 chain structure with sequence from Crithidia fasciculata. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.3Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

O96438_CRIFA

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

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1o8x"

Categories: Crithidia fasciculata | Large Structures | Alphey MS | Bond CS | Hunter WN

@@ Line 3: / Line 3: @@
 <StructureSection load='1o8x' size='340' side='right'caption='[[1o8x]], [[Resolution|resolution]] 1.30&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1o8x]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Crifa Crifa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O8X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1O8X FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1o8x]] 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=1O8X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1O8X FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1fg4|1fg4]], [[1i5g|1i5g]], [[1o6j|1o6j]], [[1o73|1o73]], [[1o81|1o81]], [[1oc8|1oc8]], [[1oc9|1oc9]], [[1ewx|1ewx]], [[1ezk|1ezk]], [[1o7u|1o7u]], [[1o85|1o85]], [[1o8w|1o8w]], [[1qk8|1qk8]]</div></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]] 1.3&#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=1o8x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o8x OCA], [https://pdbe.org/1o8x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1o8x RCSB], [https://www.ebi.ac.uk/pdbsum/1o8x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1o8x ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/O96438_CRIFA O96438_CRIFA]
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 30: / Line 32: @@
 __TOC__
 </StructureSection>
-[[Category: Crifa]]
-[[Category: Large Structures]]
-[[Category: Alphey, M S]]
-[[Category: Bond, C S]]
-[[Category: Hunter, W N]]
-[[Category: Anomalous dispersion]]
 [[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]]

1o8x

From Proteopedia

Current revision

Mutant tryparedoxin-I Cys43Ala

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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