View source for 3zij


==Crystal structure of the thioredoxin-like protein BC3987==
<StructureSection load='3zij' size='340' side='right'caption='[[3zij]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3zij]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_cereus Bacillus cereus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZIJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZIJ 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]] 1.4&#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=3zij FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zij OCA], [https://pdbe.org/3zij PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zij RCSB], [https://www.ebi.ac.uk/pdbsum/3zij PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zij ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q819J1_BACCR Q819J1_BACCR] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Thioredoxin-like proteins contain a characteristic C-x-x-C active site motif and are involved in a large number of biological processes ranging from electron transfer, cellular redox level maintenance, and regulation of cellular processes. The mechanism for deprotonation of the buried C-terminal active site cysteine in thioredoxin, necessary for dissociation of the mixed-disulfide intermediate that occurs under thiol/disulfide mediated electron transfer, is not well understood for all thioredoxin superfamily members. Here we have characterized a 8.7 kD thioredoxin (BC3987) from Bacillus cereus that unlike the typical thioredoxin appears to use the conserved Thr8 side chain near the unusual C-P-P-C active site to increase enzymatic activity by forming a hydrogen bond to the buried cysteine. Our hypothesis is based on biochemical assays and thiolate pKa titrations where the wild type and T8A mutant are compared, phylogenetic analysis of related thioredoxins, and QM/MM calculations with the BC3987 crystal structure as a precursor for modeling of reduced active sites. We suggest that our model applies to other thioredoxin subclasses with similar active site arrangements.

Tuning of thioredoxin redox properties by intramolecular hydrogen bonds.,Rohr AK, Hammerstad M, Andersson KK PLoS One. 2013 Jul 23;8(7):e69411. doi: 10.1371/journal.pone.0069411. Print 2013. PMID:23936007<ref>PMID:23936007</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3zij" style="background-color:#fffaf0;"></div>

==See Also==
*[[Thioredoxin 3D structures|Thioredoxin 3D structures]]
== References ==
<references/>
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</StructureSection>
[[Category: Bacillus cereus]]
[[Category: Large Structures]]
[[Category: Andersson KK]]
[[Category: Hammerstad M]]
[[Category: Rohr AK]]