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Protein Science, Vol 7, Issue 3 545-555, Copyright © 1998 by Cold Spring Harbor Laboratory Press

ARTICLE

Subunit asymmetry in the three-dimensional structure of a human CuZnSOD mutant found in familial amyotrophic lateral sclerosis

P. J. HART, H. LIU, M. PELLEGRINI, A. M. NERSISSIAN, E. B. GRALLA, J. S. VALENTINE and D. EISENBERG
UCLA-DOE Laboratory of Structural Biology and Molecular Medicine, University of California, Los Angeles, California 90095 Department of Chemistry and Biochemistry, University of California, Los Angeles, California 90095

The X-ray crystal structure of a human copper/zinc superoxide dismutase mutant (G37R CuZnSOD) found in some patients with the inherited form of Lou Gehrig's disease (FALS) has been determined to 1.9 A resolution. The two SOD subunits have distinct environments in the crystal and are different in structure at their copper binding sites. One subunit (subunit(intact)) shows a four-coordinate ligand geometry of the copper ion, whereas the other subunit (subunit(broken)) shows a three-coordinate geometry of the copper ion. Also, subunit(intact) displays higher atomic displacement parameters for backbone atoms ({complex}B{complex} = 30 +/- 10 A(2)) than subunit(broken) ({complex}B{complex} = 24 +/- 11 A(2)). This structure is the first CuZnSOD to show large differences between the two subunits. Factors that may contribute to these differences are discussed and a possible link of a looser structure to FALS is suggested.
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