3d22

<StructureSection load='3d22' size='340' side='right' caption='[[3d22]], [[Resolution|resolution]] 1.60&Aring;' scene=''>

<table><tr><td colspan='2'>[[3d22]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Populus_trichocarpa_x_populus_deltoides Populus trichocarpa x populus deltoides]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3D22 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3D22 FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3d21|3d21]]</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=3d22 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3d22 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3d22 RCSB], [http://www.ebi.ac.uk/pdbsum/3d22 PDBsum]</span></td></tr>

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/d2/3d22_consurf.spt"</scriptWhenChecked>

</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/chain_selection.php?pdb_ID=2ata ConSurf].

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== Publication Abstract from PubMed ==

Unlike other thioredoxins h characterized so far, a poplar thioredoxin of the h type, PtTrxh4, is reduced by glutathione and glutaredoxin (Grx) but not NADPH:thioredoxin reductase (NTR). PtTrxh4 contains three cysteines: one localized in an N-terminal extension (Cys(4)) and two (Cys(58) and Cys(61)) in the classical thioredoxin active site ((57)WCGPC(61)). The property of a mutant in which Cys(58) was replaced by serine demonstrates that it is responsible for the initial nucleophilic attack during the catalytic cycle. The observation that the C4S mutant is inactive in the presence of Grx but fully active when dithiothreitol is used as a reductant indicates that Cys(4) is required for the regeneration of PtTrxh4 by Grx. Biochemical and x-ray crystallographic studies indicate that two intramolecular disulfide bonds involving Cys(58) can be formed, linking it to either Cys(61) or Cys(4). We propose thus a four-step disulfide cascade mechanism involving the transient glutathionylation of Cys(4) to convert this atypical thioredoxin h back to its active reduced form.

An atypical catalytic mechanism involving three cysteines of thioredoxin.,Koh CS, Navrot N, Didierjean C, Rouhier N, Hirasawa M, Knaff DB, Wingsle G, Samian R, Jacquot JP, Corbier C, Gelhaye E J Biol Chem. 2008 Aug 22;283(34):23062-72. Epub 2008 Jun 14. PMID:18552403<ref>PMID:18552403</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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*[[Thioredoxin|Thioredoxin]]

[[Category: Populus trichocarpa x populus deltoides]]

[[Category: Corbier, C]]

[[Category: Didierjean, C]]

[[Category: Gelhaye, E]]

[[Category: Jacquot, J P]]

[[Category: Koh, C S]]

[[Category: Rouhier, N]]

[[Category: Transport]]