1sda

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

File:1sda.gif


1sda, resolution 2.5Å

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OverviewOverview

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.

About this StructureAbout this Structure

1SDA is a Single protein structure of sequence from Bos taurus with NO2, CU, ZN and ACE as ligands. Active as Superoxide dismutase, with EC number 1.15.1.1 Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of peroxynitrite-modified bovine Cu,Zn superoxide dismutase., Smith CD, Carson M, van der Woerd M, Chen J, Ischiropoulos H, Beckman JS, Arch Biochem Biophys. 1992 Dec;299(2):350-5. PMID:1444476

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