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1BEX

STRUCTURE OF RUTHENIUM-MODIFIED PSEUDOMONAS AERUGINOSA AZURIN

Summary for 1BEX
Entry DOI10.2210/pdb1bex/pdb
DescriptorAZURIN, COPPER (II) ION, RUTHEMIUM BIS(2,2'-BIPYRIDINE)-2-IMIDAZOLE, ... (4 entities in total)
Functional Keywordsazurin, electron transport
Biological sourcePseudomonas aeruginosa
Cellular locationPeriplasm: P00282
Total number of polymer chains2
Total formula weight29140.81
Authors
Faham, S.,Day, M.W.,Rees, D.C. (deposition date: 1998-05-18, release date: 1998-10-14, Last modification date: 2024-11-13)
Primary citationFaham, S.,Day, M.W.,Connick, W.B.,Crane, B.R.,Di Bilio, A.J.,Schaefer, W.P.,Rees, D.C.,Gray, H.B.
Structures of ruthenium-modified Pseudomonas aeruginosa azurin and [Ru(2,2'-bipyridine)2(imidazole)2]SO4 x 10H2O.
Acta Crystallogr.,Sect.D, 55:379-385, 1999
Cited by
PubMed Abstract: The 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.
PubMed: 10089343
DOI: 10.1107/S0907444998010464
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.3 Å)
Structure validation

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