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1YSO

YEAST CU, ZN SUPEROXIDE DISMUTASE WITH THE REDUCED BRIDGE BROKEN

Summary for 1YSO
Entry DOI10.2210/pdb1yso/pdb
DescriptorYEAST CU, ZN SUPEROXIDE DISMUTASE, COPPER (I) ION, ZINC ION, ... (4 entities in total)
Functional Keywordsoxidoreductase (superoxide acceptor), copper, zinc
Biological sourceCandida albicans
Cellular locationCytoplasm : P00445
Total number of polymer chains1
Total formula weight15872.34
Authors
Parge, H.E.,Crane, B.R.,Tsang, J.,Tainer, J.A. (deposition date: 1995-12-21, release date: 1996-06-10, Last modification date: 2024-10-09)
Primary citationOgihara, N.L.,Parge, H.E.,Hart, P.J.,Weiss, M.S.,Goto, J.J.,Crane, B.R.,Tsang, J.,Slater, K.,Roe, J.A.,Valentine, J.S.,Eisenberg, D.,Tainer, J.A.
Unusual trigonal-planar copper configuration revealed in the atomic structure of yeast copper-zinc superoxide dismutase.
Biochemistry, 35:2316-2321, 1996
Cited by
PubMed 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 angstrom 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 angstrom resolution range and 18. 2% for 17 682 reflections (F > 2 sigma) in the 10.0-1.73 angstrom resolution range. A third structure has been determined using X-ray data collected at -180 degrees 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 angstrom 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.
PubMed: 8652572
DOI: 10.1021/bi951930b
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.73 Å)
Structure validation

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