1bex | pdb_00001bex
STRUCTURE OF RUTHENIUM-MODIFIED PSEUDOMONAS AERUGINOSA AZURIN
Structural highlights
FunctionAZUR_PSEAE Transfers electrons from cytochrome c551 to cytochrome 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 PubMedThe crystal structure of Ru(2, 2'-bipyridine)2(imidazole)(His83)azurin (RuAz) has been determined to 2.3 A -resolution by X-ray crystallography. The spectroscopic and thermodynamic properties of both the native protein and [Ru(2, 2'-bipyridine)2(imidazole)2]2+ are maintained in the modified protein. Dark-green RuAz crystals grown from PEG 4000, LiNO3, CuCl2 and Tris buffer are monoclinic, belong to the space group C2 and have cell parameters a = 100.6, b = 35.4, c = 74.7 A and beta = 106. 5 degrees. In addition, [Ru(2,2'-bipyridine)2(imidazole)2]SO4 x 10H2O was synthesized, crystallized and structurally characterized by X-ray crystallography. Red-brown crystals of this complex are monoclinic, space group P21/n, unit-cell parameters a = 13.230 (2), b = 18.197 (4), c = 16.126 (4) A, beta = 108.65 (2) degrees. Stereochemical parameters for the refinement of Ru(2, 2'-bipyridine)2(imidazole)(His83) were taken from the atomic coordinates of [Ru(2,2'-bipyridine)2(imidazole)2]2+. The structure of RuAz confirms that His83 is the only site of chemical modification and that the native azurin structure is not perturbed significantly by the ruthenium label. Structures of ruthenium-modified Pseudomonas aeruginosa azurin and [Ru(2,2'-bipyridine)2(imidazole)2]SO4 x 10H2O.,Faham S, Day MW, Connick WB, Crane BR, Di Bilio AJ, Schaefer WP, Rees DC, Gray HB Acta Crystallogr D Biol Crystallogr. 1999 Feb;55(Pt 2):379-85. PMID:10089343[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences | ||||||||||||||||||||
