2cak

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spinqualitylabelsall models 2cak, resolution 1.27Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

1.27ANGSTROM STRUCTURE OF RUSTICYANIN FROM THIOBACILLUS FERROOXIDANS

Overview

Rusticyanin from the extremophile Thiobacillus ferrooxidans is a blue, copper protein with unusually high redox potential and acid stability. We, present the crystal structures of native rusticyanin and of its Cu site, mutant His143Met at 1.27 and 1.10 A, respectively. The very high, resolution of these structures allows a direct comparison with EXAFS data, and with quantum chemical models of the oxidized and reduced forms of the, proteins, based upon both isolated and embedded clusters and density, functional theory (DFT) methods. We further predict the structure of the, Cu(II) form of the His143Met mutant which has been experimentally, inaccessible due to its very high redox potential. We also present, metrical EXAFS data and quantum chemical calculations for the oxidized and, reduced ... [(full description)]

About this Structure

2CAK is a [Single protein] structure of sequence from [[1]] with CU1 as [ligand]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

Reference

Atomic resolution crystal structures, EXAFS, and quantum chemical studies of rusticyanin and its two mutants provide insight into its unusual properties., Barrett ML, Harvey I, Sundararajan M, Surendran R, Hall JF, Ellis MJ, Hough MA, Strange RW, Hillier IH, Hasnain SS, Biochemistry. 2006 Mar 7;45(9):2927-39. PMID:16503647

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