4hu9

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{{STRUCTURE_4hu9| PDB=4hu9 | SCENE= }}
 
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===E. coli thioredoxin variant with (4S)-FluoroPro76 as single proline residue===
 
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{{ABSTRACT_PUBMED_23712956}}
 
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==Function==
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==E. coli thioredoxin variant with (4S)-FluoroPro76 as single proline residue==
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[[http://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.
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<StructureSection load='4hu9' size='340' side='right'caption='[[4hu9]], [[Resolution|resolution]] 1.55&Aring;' scene=''>
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== Structural highlights ==
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<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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.55&#8491;</td></tr>
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<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>
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<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>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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==About this Structure==
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(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>
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[[4hu9]] is a 1 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=4HU9 OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<ref group="xtra">PMID:023712956</ref><references group="xtra"/><references/>
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</div>
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[[Category: Escherichia coli k-12]]
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<div class="pdbe-citations 4hu9" style="background-color:#fffaf0;"></div>
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[[Category: Capitani, G.]]
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[[Category: Glockshuber, R.]]
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==See Also==
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[[Category: Rubini, M.]]
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*[[Thioredoxin 3D structures|Thioredoxin 3D structures]]
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[[Category: Scharer, M A.]]
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== References ==
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[[Category: 4s-fluoroproline]]
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<references/>
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[[Category: Cisproline]]
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__TOC__
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[[Category: Oxidoreductase]]
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</StructureSection>
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[[Category: Protein disulfide oxidoreductase activity]]
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[[Category: Escherichia coli K-12]]
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[[Category: Thioredoxin fold]]
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[[Category: Large Structures]]
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[[Category: Capitani G]]
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[[Category: Glockshuber R]]
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[[Category: Rubini M]]
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[[Category: Scharer MA]]

Current revision

E. coli thioredoxin variant with (4S)-FluoroPro76 as single proline residue

PDB ID 4hu9

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