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==NMR-structure of tryparedoxin 1==
==NMR-structure of tryparedoxin 1==
<StructureSection load='1okd' size='340' side='right'caption='[[1okd]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
<StructureSection load='1okd' size='340' side='right'caption='[[1okd]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1okd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Crifa Crifa]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OKD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OKD FirstGlance]. <br>
<table><tr><td colspan='2'>[[1okd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Crithidia_fasciculata Crithidia fasciculata]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OKD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OKD 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;'>[[1ewx|1ewx]], [[1ezk|1ezk]], [[1o7u|1o7u]], [[1o85|1o85]], [[1o8w|1o8w]], [[1o8x|1o8x]], [[1qk8|1qk8]]</div></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1okd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1okd OCA], [https://pdbe.org/1okd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1okd RCSB], [https://www.ebi.ac.uk/pdbsum/1okd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1okd 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=1okd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1okd OCA], [https://pdbe.org/1okd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1okd RCSB], [https://www.ebi.ac.uk/pdbsum/1okd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1okd ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/O96438_CRIFA O96438_CRIFA]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</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=1okd ConSurf].
</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=1okd ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Tryparedoxins (TXNs) are trypanothione-dependent peroxiredoxin oxidoreductases involved in hydroperoxide detoxification that have been shown to determine virulence in trypanosomatids. The structure of (15)N,(13)C-doubly-labeled, C-terminally-His-tagged tryparedoxin 1 from Crithidia fasciculata (Cf TXN1) was elucidated by three-dimensional NMR spectroscopy. Global folding was found to be similar to the crystal structure, but regions near the active site, especially the onset of helix alpha1 with the redox-active Cys 43 and helix alpha2 relevant to substrate binding, were less well defined in solution. The redox-inactive inhibitory substrate analogue N(1),N(8)-bis(ophthalmyl)spermidine was used to study the substrate/TXN interaction by two-dimensional (1)H,(15)N NMR spectroscopy. The NMR data complemented by molecular modeling revealed several alternative modes of ligand binding. The results confirm and extend the concept of TXN action and specificity derived from X-ray analysis and site-directed mutagenesis and thus improve the rational basis for inhibitor design.
NMR studies of the interaction of tryparedoxin with redox-inactive substrate homologues.,Krumme D, Budde H, Hecht HJ, Menge U, Ohlenschlager O, Ross A, Wissing J, Wray V, Flohe L Biochemistry. 2003 Dec 23;42(50):14720-8. PMID:14674746<ref>PMID:14674746</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1okd" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Crifa]]
[[Category: Crithidia fasciculata]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Budde, H]]
[[Category: Budde H]]
[[Category: Flohe, L]]
[[Category: Flohe L]]
[[Category: Hecht, H J]]
[[Category: Hecht H-J]]
[[Category: Krumme, D]]
[[Category: Krumme D]]
[[Category: Menge, U]]
[[Category: Menge U]]
[[Category: Ohlenschlager, O]]
[[Category: Ohlenschlager O]]
[[Category: Ross, A]]
[[Category: Ross A]]
[[Category: Wissing, J]]
[[Category: Wissing J]]
[[Category: Wray, V]]
[[Category: Wray V]]
[[Category: Electron transport]]
[[Category: Nmr spectroscopy]]
[[Category: Trypanosomatid]]
[[Category: Tryparedoxin]]

Revision as of 05:48, 17 April 2024

NMR-structure of tryparedoxin 1

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