The structure and dynamics in solution of Cu(I) pseudoazurin from Paracoccus pantotrophus

Gary S. Thompson, Yun Chung Leung, Stuart J. Ferguson, Sheena E. Radford, Christina Redfield

Research output: Journal article publicationJournal articleAcademic researchpeer-review

19 Citations (Scopus)


The solution structure and backbone dynamics of Cu(I) pseudoazurin, a 123 amino acid electron transfer protein from Paracoccus pantotrophus, have been determined using NMR methods. The structure was calculated to high precision, with a backbone RMS deviation for secondary structure elements of 0.35 ± 0.06 Å, using 1,498 distance and 55 torsion angle constraints. The protein has a double-wound Greek-key fold with two α-helices toward its C- terminus, similar to that of its oxidized counterpart determined by X-ray crystallography. Comparison of the Cu(I) solution structure with the X-ray structure of the Cu(II) protein shows only small differences in the positions of some of the secondary structure elements. Order parameters S2, measured for amide nitrogens, indicate that the backbone of the protein is rigid on the picosecond to nanosecond timescale.
Original languageEnglish
Pages (from-to)846-858
Number of pages13
JournalProtein Science
Issue number5
Publication statusPublished - 1 Jan 2000


  • Backbone dynamics
  • Cupredoxins
  • Electron transfer
  • Nuclear magnetic resonance
  • Pseudoazurin

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

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