Abstract
The three-dimensional structure of yeast copper-zinc superoxide dismutase (CuZnSOD) has been determined in a new crystal form in space group R32 and refined against X-ray diffraction data using difference Fourier and restrained crystallographic refinement techniques. The unexpected result is that the copper ion has moved approximately 1 Å from its position in previously reported CuZnSOD models, the copper-imidazolate bridge is broken, and a roughly trigonal planar ligand geometry characteristic of Cu(I) rather than Cu(II) is revealed. Final R values for the two nearly identical room temperature structures are 18.6% for all 19 149 reflections in the 10.0-1.7 Å resolution range and 18.2% for 17 682 reflections (F > 2σ) in the 10.0- 1.73 Å resolution range. A third structure has been determined using X-ray data collected at -180 °C. The final R value for this structure is 19.0% (R(free) = 22.9%) for all 24 356 reflections in the 10.0-1.55 Å resolution range. Virtually no change in the positions of the ligands to the zinc center is observed in these models. The origin of the broken bridge and altered Cu- ligand geometry is discussed.
Original language | English (US) |
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Pages (from-to) | 2316-2321 |
Number of pages | 6 |
Journal | Biochemistry |
Volume | 35 |
Issue number | 7 |
DOIs | |
State | Published - Feb 20 1996 |
ASJC Scopus subject areas
- Biochemistry