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Title(4R)- and (4S)-Fluoroproline in the Conserved cis-Prolyl Peptide Bond of the Thioredoxin Fold: Tertiary Structure Context Dictates Ring Puckering.
Journal, issue, pagesChembiochem, Vol. 14, Page 1053-1057, Year 2013
Publish dateNov 2, 2012 (structure data deposition date)
AuthorsRubini, M. / Scharer, M.A. / Capitani, G. / Glockshuber, R.
External linksChembiochem / PubMed:23712956
MethodsX-ray diffraction
Resolution1.1 - 1.55 Å
Structure data

PDB-4hu7:
E. coli thioredoxin variant with Pro76 as single proline residue
Method: X-RAY DIFFRACTION / Resolution: 1.4 Å

PDB-4hu9:
E. coli thioredoxin variant with (4S)-FluoroPro76 as single proline residue
Method: X-RAY DIFFRACTION / Resolution: 1.55 Å

PDB-4hua:
E. coli thioredoxin variant with (4R)-FluoroPro76 as single proline residue
Method: X-RAY DIFFRACTION / Resolution: 1.1 Å

Chemicals

ChemComp-CU:
COPPER (II) ION

ChemComp-NA:
Unknown entry

ChemComp-HOH:
WATER

Source
  • escherichia coli (E. coli)
KeywordsOXIDOREDUCTASE / cisproline / Thioredoxin fold / protein disulfide oxidoreductase activity / 4s-fluoroproline / 4r-fluoroproline

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