4HU7

E. coli thioredoxin variant with Pro76 as single proline residue

Summary for 4HU7

• Entry DOI: 10.2210/pdb4hu7/pdb
• Related: 4HU9 4HUA
• Descriptor: Thioredoxin-1, COPPER (II) ION, SODIUM ION, ... (4 entities in total)
• Functional Keywords: cisproline, thioredoxin fold, protein disulfide oxidoreductase activity, oxidoreductase
• Biological source: Escherichia coli
• Total number of polymer chains: 2
• Total formula weight: 23316.56

Authors

Glockshuber, R.,Scharer, M.A.,Capitani, G.,Rubini, M. (deposition date: 2012-11-02, release date: 2013-05-29, Last modification date: 2024-11-20)

Primary citation

Rubini, M.,Scharer, M.A.,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, 14:1053-1057, 2013

PubMed Abstract: 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.

PubMed: 23712956
DOI: 10.1002/cbic.201300178

Experimental method

X-RAY DIFFRACTION (1.4 Å)