1Q0E

Atomic resolution (1.15 ) crystal structure of bovine copper, zinc superoxide dismutase

Summary for 1Q0E

• Entry DOI: 10.2210/pdb1q0e/pdb
• Descriptor: Superoxide dismutase [Cu-Zn], COPPER (II) ION, ZINC ION, ... (4 entities in total)
• Functional Keywords: bovine, superoxide dismutase, atomic resolution, copper, zinc, oxidoreductase, metal binding protein
• Biological source: Bos taurus (cattle)
• Cellular location: Cytoplasm: P00442
• Total number of polymer chains: 2
• Total formula weight: 31456.66

Authors

Hough, M.A.,Hasnain, S.S. (deposition date: 2003-07-16, release date: 2003-09-23, Last modification date: 2024-10-16)

Primary citation

Hough, M.A.,Hasnain, S.S.
Structure of fully reduced bovine copper zinc superoxide dismutase at 1.15 A.
Structure, 11:937-946, 2003

PubMed Abstract: Copper zinc superoxide dismutase (CuZnSOD) forms a crucial component of the cellular response to oxidative stress by catalyzing the dismutation of the superoxide radical to hydrogen peroxide and water. Mutations in human CuZnSOD are associated with the development of familial amyotrophic lateral sclerosis (motor neuron disease). We have determined the structure of fully reduced bovine CuZnSOD to 1.15 A, the only atomic resolution structure for an intact CuZnSOD and one of only a small number for metalloproteins. For the first time, both subunits have been captured with the three coordinate Cu(I) ligation required by the generally accepted catalytic mechanism, where dismutation of the superoxide radical occurs via reduction of Cu. Furthermore, the improved resolution compared to previous studies (to 1.65 A) has allowed a more detailed examination of the metal center environment and its associated water network in the active site channel, facilitating the analysis of potential proton transfer routes.

PubMed: 12906825
DOI: 10.1016/S0969-2126(03)00155-2

Experimental method

X-RAY DIFFRACTION (1.15 Å)