4hu7: Difference between revisions

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<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>
<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>
</table>
== Function ==
[[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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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==

Revision as of 01:31, 26 December 2014

E. coli thioredoxin variant with Pro76 as single proline residueE. coli thioredoxin variant with Pro76 as single proline residue

Structural highlights

4hu7 is a 2 chain structure with sequence from Escherichia coli k-12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:,
Gene:trxA (Escherichia coli K-12)
Resources:FirstGlance, OCA, RCSB, PDBsum

Function

[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.

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Rubini M, Scharer MA, Capitani G, Glockshuber R. (4R)- and (4S)-Fluoroproline in the Conserved cis-Prolyl Peptide Bond of the Thioredoxin Fold: Tertiary Structure Context Dictates Ring Puckering. Chembiochem. 2013 Jun 17;14(9):1053-7. doi: 10.1002/cbic.201300178. Epub 2013 May, 27. PMID:23712956 doi:10.1002/cbic.201300178

4hu7, resolution 1.40Å

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