View source for 4xhm


==Archaeoglobus fulgidus thioredoxin 3 M60H==
<StructureSection load='4xhm' size='340' side='right'caption='[[4xhm]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4xhm]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Archaeoglobus_fulgidus_DSM_4304 Archaeoglobus fulgidus DSM 4304]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XHM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4XHM 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]] 1.95&#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=4xhm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xhm OCA], [https://pdbe.org/4xhm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4xhm RCSB], [https://www.ebi.ac.uk/pdbsum/4xhm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4xhm ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/O28984_ARCFU O28984_ARCFU] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Thioredoxins are small soluble proteins that contain a redox-active disulfide (CXXC). These disulfides are tuned to oxidizing or reducing potentials depending on the function of the thioredoxin within the cell. The mechanism by which the potential is tuned has been controversial, with two main hypotheses: first, that redox potential (Em) is specifically governed by a molecular 'rheostat'-the XX amino acids, which influence the Cys pKa values, and thereby, Em; and second, the overall thermodynamics of protein folding stability regulates the potential. Here, we use protein film voltammetry (PFV) to measure the pH dependence of the redox potentials of a series of wild-type and mutant archaeal Trxs, PFV and glutathionine-equilibrium to corroborate the measured potentials, the fluorescence probe BADAN to measure pKa values, guanidinium-based denaturation to measure protein unfolding, and X-ray crystallography to provide a structural basis for our functional analyses. We find that when these archaeal thioredoxins are probed directly using PFV, both the high and low potential thioredoxins display consistent 2H+:2e- coupling over a physiological pH range, in conflict with the conventional 'rheostat' model. Instead, folding measurements reveals an excellent correlation to reduction potentials, supporting the second hypothesis and revealing the molecular mechanism of reduction potential control in the ubiquitous Trx family.

Rheostat re-wired: alternative hypotheses for the control of thioredoxin reduction potentials.,Bewley KD, Dey M, Bjork RE, Mitra S, Chobot SE, Drennan CL, Elliott SJ PLoS One. 2015 Apr 13;10(4):e0122466. doi: 10.1371/journal.pone.0122466., eCollection 2015. PMID:25874934<ref>PMID:25874934</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4xhm" style="background-color:#fffaf0;"></div>

==See Also==
*[[Thioredoxin 3D structures|Thioredoxin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Archaeoglobus fulgidus DSM 4304]]
[[Category: Large Structures]]
[[Category: Bjork RE]]
[[Category: Dey M]]
[[Category: Drennan CL]]