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4hua
From Proteopedia
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| - | {{STRUCTURE_4hua| PDB=4hua | SCENE= }} | ||
| - | ===E. coli thioredoxin variant with (4R)-FluoroPro76 as single proline residue=== | ||
| - | {{ABSTRACT_PUBMED_23712956}} | ||
| - | == | + | ==E. coli thioredoxin variant with (4R)-FluoroPro76 as single proline residue== |
| - | [[http://www.uniprot.org/uniprot/THIO_ECOLI THIO_ECOLI | + | <StructureSection load='4hua' size='340' side='right'caption='[[4hua]], [[Resolution|resolution]] 1.10Å' 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]] 1.1Å</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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | < | + | </div> |
| - | [[Category: Escherichia coli | + | <div class="pdbe-citations 4hua" style="background-color:#fffaf0;"></div> |
| - | [[Category: | + | |
| - | [[Category: | + | ==See Also== |
| - | [[Category: | + | *[[Thioredoxin 3D structures|Thioredoxin 3D structures]] |
| - | [[Category: | + | == References == |
| - | [[Category: | + | <references/> |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
| - | + | [[Category: Escherichia coli K-12]] | |
| - | + | [[Category: Large Structures]] | |
| + | [[Category: Capitani G]] | ||
| + | [[Category: Glockshuber R]] | ||
| + | [[Category: Rubini M]] | ||
| + | [[Category: Scharer MA]] | ||
Current revision
E. coli thioredoxin variant with (4R)-FluoroPro76 as single proline residue
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