2cak | pdb_00002cak

1.27Angstrom Structure of Rusticyanin from Thiobacillus ferrooxidans

spinqualitylabelsall models 2cak, resolution 1.27Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2cak is a 1 chain structure with sequence from Acidithiobacillus ferrooxidans. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.27Å Ligands: CU1 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function RUS2_ACIFI Electron carrier from cytochrome c552 to the A-type oxidase. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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 states of the Met148Gln mutant, this protein having the lowest redox potential of all currently characterized mutants of rusticyanin. These data offer new insights into the structural factors which affect the redox potential in this important class of proteins. Calculations successfully predict the structure and the order of redox potentials for the three proteins. The calculated redox potential of H143M ( approximately 400 mV greater than native rusticyanin) is consistent with the failure of readily available chemical oxidants to restore a Cu(II) species of this mutant. The structural and energetic effects of mutating the equatorial cysteine to serine, yet to be studied experimentally, are predicted to be considerable by our calculations. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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