1SDA

CRYSTAL STRUCTURE OF PEROXYNITRITE-MODIFIED BOVINE CU,ZN SUPEROXIDE DISMUTASE

Summary for 1SDA

• Entry DOI: 10.2210/pdb1sda/pdb
• Descriptor: COPPER,ZINC SUPEROXIDE DISMUTASE, COPPER (II) ION, ZINC ION, ... (4 entities in total)
• Functional Keywords: oxidoreductase(copper)
• Biological source: Bos taurus (cattle)
• Cellular location: Cytoplasm: P00442
• Total number of polymer chains: 4
• Total formula weight: 63093.30

Authors

Smith, C.D.,Carson, M.,Van Der Woerd, M.,Chen, J.,Ischiropoulos, H.,Beckman, J.S. (deposition date: 1993-01-13, release date: 1993-10-31, Last modification date: 2017-11-29)

Primary citation

Smith, C.D.,Carson, M.,van der Woerd, M.,Chen, J.,Ischiropoulos, H.,Beckman, J.S.
Crystal structure of peroxynitrite-modified bovine Cu,Zn superoxide dismutase.
Arch.Biochem.Biophys., 299:350-355, 1992

PubMed Abstract: The crystal structure of bovine Cu,Zn superoxide dismutase modified with peroxynitrite (ONOO-) was determined by X-ray diffraction, utilizing the existing three-dimensional model of the native structure deposited in the Brookhaven Protein Data Bank (J. A. Tainer et al., J. Mol. Biol. 160, 181-217, 1982). The native structure and the modified derivative were refined to R factors of 19.0 and 18.7% respectively using diffraction data from 6.0 to 2.5 A. The major result after reaction with peroxynitrite was the appearance of electron density 1.45 A from a single epsilon carbon of Tyr-108, the only tyrosine residue in the sequence. Tyr-108 is a solvent-exposed residue 18 A from the copper atom in the active site. The electron density was consistent with nitration of Tyr-108 at one of the epsilon carbons to form 3-nitrotyrosine. We propose that the nitration occurs in solution by transfer of a nitronium-like species from the active site on one superoxide dismutase dimer to the Tyr-108 of a second dimer.

PubMed: 1444476
DOI: 10.1016/0003-9861(92)90286-6

Experimental method

X-RAY DIFFRACTION (2.5 Å)