1bqr
From Proteopedia
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REDUCED PSEUDOAZURIN
Overview
The crystal structures of oxidized and reduced pseudoazurins from a, denitrifying bacterium, Achromobacter cycloclastes IAM1013, have been, determined at 1.35- and 1.6-A 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 A, between N-delta1(His6) and O-gamma1(Thr36) in the oxidized protein. When, the protein is reduced at pH 6.0, the imidazole ring rotates by 30.3, degrees and moves 1.00 A away from the position of the oxidized state. A, new hydrogen bond between N-epsilon2(His6) and O-epsilon1(Glu4) is formed, with a distance of 3.03 A, while the hydrogen bond between, N-delta1(His6)-O-gamma1(Thr36) is maintained with an interatomic distance, of 2.81 A. A concomitant peptide bond flip of main chain between Ile34 and, Thr36 occurs.
About this Structure
1BQR is a Single protein structure of sequence from Achromobacter cycloclastes with CU as ligand. Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
Crystal structure determinations of oxidized and reduced pseudoazurins from Achromobacter cycloclastes. Concerted movement of copper site in redox forms with the rearrangement of hydrogen bond at a remote histidine., Inoue T, Nishio N, Suzuki S, Kataoka K, Kohzuma T, Kai Y, J Biol Chem. 1999 Jun 18;274(25):17845-52. PMID:10364229
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