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 [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4HU7 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4hua|4hua]], [[4hu9|4hu9]]</td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">trxA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 Escherichia coli K-12])</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4hu7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hu7 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4hu7 RCSB], [http://www.ebi.ac.uk/pdbsum/4hu7 PDBsum]</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> | |||
== | ==See Also== | ||
*[[Thioredoxin|Thioredoxin]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Escherichia coli k-12]] | [[Category: Escherichia coli k-12]] | ||
[[Category: Capitani, G | [[Category: Capitani, G]] | ||
[[Category: Glockshuber, R | [[Category: Glockshuber, R]] | ||
[[Category: Rubini, M | [[Category: Rubini, M]] | ||
[[Category: Scharer, M A | [[Category: Scharer, M A]] | ||
[[Category: Cisproline]] | [[Category: Cisproline]] | ||
[[Category: Oxidoreductase]] | [[Category: Oxidoreductase]] | ||
[[Category: Protein disulfide oxidoreductase activity]] | [[Category: Protein disulfide oxidoreductase activity]] | ||
[[Category: Thioredoxin fold]] | [[Category: Thioredoxin fold]] | ||
Revision as of 15:25, 21 December 2014
E. coli thioredoxin variant with Pro76 as single proline residueE. coli thioredoxin variant with Pro76 as single proline residue
Structural highlights
Publication Abstract from PubMedFine-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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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