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

Thompson, GS, Radford, SE, Leung, Y-C, Redfield, C, Ferguson, SJ (2000) The structure and dynamics in solution of Cu(I) pseudoazurin from Paracoccus pantotrophus. Protein Science, 9 . pp. 846-858. ISSN 0961-8368. (doi:10.1110/ps.9.5.846) (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided)

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http://dx.doi.org/10.1110/ps.9.5.846

Abstract

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 A, using 1,498 distance and 55 torsion angle constraints. The protein has a double-wound Greek-key fold with two alpha-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.

Item Type: Article
DOI/Identification number: 10.1110/ps.9.5.846
Subjects: Q Science > QD Chemistry > QD431 Organic Chemistry- Biochemistry- Proteins, peptides, amino acids
Q Science > QP Physiology (Living systems) > QP506 Molecular biology
Q Science > QP Physiology (Living systems) > QP517 Biochemistry
Divisions: Faculties > Sciences > School of Biosciences
Depositing User: G. Thompson
Date Deposited: 23 Jan 2019 16:32 UTC
Last Modified: 30 May 2019 08:47 UTC
Resource URI: https://kar.kent.ac.uk/id/eprint/71828 (The current URI for this page, for reference purposes)
Thompson, GS: https://orcid.org/0000-0001-9399-7636
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