View source for 4hua


==E. coli thioredoxin variant with (4R)-FluoroPro76 as single proline residue==
<StructureSection load='4hua' size='340' side='right'caption='[[4hua]], [[Resolution|resolution]] 1.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4hua]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HUA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4HUA 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]] 1.1&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=FP9:(4R)-4-FLUORO-L-PROLINE'>FP9</scene></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=4hua FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hua OCA], [https://pdbe.org/4hua PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4hua RCSB], [https://www.ebi.ac.uk/pdbsum/4hua PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4hua ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/THIO_ECOLI THIO_ECOLI] Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Fine-tuning protein stability: The non-natural amino acids (2S,4R)- and (2S,4S)-fluoroproline modulate protein stability by biasing the proline ring pucker and the cis/trans equilibrium of prolyl peptide bonds. We incorporated both fluoroproline stereoisomers at the invariant cis-proline residue of the thioredoxin fold. The results show that tertiary structure context overrules the conformational preferences of fluoroprolines.

(4R)- and (4S)-Fluoroproline in the Conserved cis-Prolyl Peptide Bond of the Thioredoxin Fold: Tertiary Structure Context Dictates Ring Puckering.,Rubini M, Scharer MA, Capitani G, Glockshuber R Chembiochem. 2013 Jun 17;14(9):1053-7. doi: 10.1002/cbic.201300178. Epub 2013 May, 27. PMID:23712956<ref>PMID:23712956</ref>

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

==See Also==
*[[Thioredoxin 3D structures|Thioredoxin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli K-12]]
[[Category: Large Structures]]
[[Category: Capitani G]]
[[Category: Glockshuber R]]
[[Category: Rubini M]]
[[Category: Scharer MA]]