Crystal Structure Determinations of Oxidized and Reduced Pseudoazurins from Achromobacter cycloclastes

The crystal structures of oxidized and reduced pseudoazurins from a denitrifying bacterium, Achromobacter cycloclastes IAM1013, have been determined at 1.35- and 1.6-Å resolutions, respectively. The copper site in the oxidized state exhibits a distorted tetrahedral structure like those of other pseudoazurins. However, not only a small change of the copper geometry, but concerted peptide bond flips are identified. The imidazole ring of remote His6 has a hydrogen bonding distance of 2.73 Å between N-δ1(His6) and O-γ1(Thr36) in the oxidized protein. When the protein is reduced at pH 6.0, the imidazole ring rotates by 30.3° and moves 1.00 Å away from the position of the oxidized state. A new hydrogen bond between N-ε2(His6) and O-ε1(Glu4) is formed with a distance of 3.03 Å, while the hydrogen bond between N-δ1(His6)-O-γ1(Thr36) is maintained with an interatomic distance of 2.81 Å. A concomitant peptide bond flip of main chain between Ile34 and Thr36 occurs.

• Publication year

  1999

• Venue

  Journal of Biological Chemistry

• Publication date

  1999-06-18

• Fields of study

  Biology, Medicine, Chemistry, Environmental Science

• Identifiers
  DOI 10.1074/jbc.274.25.17845PMID 10364229
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

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