4hu9
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==E. coli thioredoxin variant with (4S)-FluoroPro76 as single proline residue== | |
| + | <StructureSection load='4hu9' size='340' side='right'caption='[[4hu9]], [[Resolution|resolution]] 1.55Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4hu9]] 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=4HU9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4HU9 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]] 1.55Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=4FB:(4S)-4-FLUORO-L-PROLINE'>4FB</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</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=4hu9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hu9 OCA], [https://pdbe.org/4hu9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4hu9 RCSB], [https://www.ebi.ac.uk/pdbsum/4hu9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4hu9 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <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 4hu9" 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]] | ||
Current revision
E. coli thioredoxin variant with (4S)-FluoroPro76 as single proline residue
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