4HUA

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

Summary for 4HUA

Entry DOI	10.2210/pdb4hua/pdb
Related	4HU7 4HU9
Descriptor	Thioredoxin-1, COPPER (II) ION (3 entities in total)
Functional Keywords	4r-fluoroproline, cisproline, thioredoxin fold, protein disulfide oxidoreductase activity, oxidoreductase
Biological source	Escherichia coli
Total number of polymer chains	1
Total formula weight	11664.77
Authors	Scharer, M.A.,Rubini, M.,Capitani, G.,Glockshuber, R. (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 Cited by 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 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.1 Å)

Structure validation