4hu7: Difference between revisions
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==E. coli thioredoxin variant with Pro76 as single proline residue== | |||
<StructureSection load='4hu7' size='340' side='right'caption='[[4hu7]], [[Resolution|resolution]] 1.40Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4hu7]] is a 2 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=4HU7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4HU7 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]] 1.4Å</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=NA:SODIUM+ION'>NA</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=4hu7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hu7 OCA], [https://pdbe.org/4hu7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4hu7 RCSB], [https://www.ebi.ac.uk/pdbsum/4hu7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4hu7 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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4hu7" 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]] | |||
Latest revision as of 15:11, 20 September 2023
E. coli thioredoxin variant with Pro76 as single proline residue
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