4hu7: Difference between revisions

← Older edit

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 4hu7 is ON HOLD
+==E. coli thioredoxin variant with Pro76 as single proline residue==
+<StructureSection load='4hu7' size='340' side='right'caption='[[4hu7]], [[Resolution|resolution]] 1.40&Aring;' 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]] 1.4&#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=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.
-Authors: Glockshuber, R., Scharer, M.A., Rubini, M.
+(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>
-Description: E. coli thioredoxin variant with Pro76 as single proline residue
+From MEDLINE&reg;/PubMed&reg;, 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]]