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Structural and dynamic aspects related to oligomerization of apo SOD1 and its mutants.

Banci L, Bertini I, Boca M, Calderone V, Cantini F, Girotto S, Vieru M
Proc Natl Acad Sci U S A 106 6980-5 (2009)
Related entries: 3ecu, 3ecw

Cited: 73 times
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Abstract

The structural and dynamical properties of the metal-free form of WT human superoxide dismutase 1 (SOD1) and its familial amyotrophic lateral sclerosis (fALS)-related mutants, T54R and I113T, were characterized both in solution, through NMR, and in the crystal, through X-ray diffraction. We found that all 3 X-ray structures show significant structural disorder in 2 loop regions that are, at variance, well defined in the fully-metalated structures. Interestingly, the apo state crystallizes only at low temperatures, whereas all 3 proteins in the metalated form crystallize at any temperature, suggesting that crystallization selects one of the most stable conformations among the manifold adopted by the apo form in solution. Indeed, NMR experiments show that the protein in solution is highly disordered, sampling a large range of conformations. The large conformational variability of the apo state allows the free reduced cysteine Cys-6 to become highly solvent accessible in solution, whereas it is essentially buried in the metalated state and the crystal structures. Such solvent accessibility, together with that of Cys-111, accounts for the tendency to oligomerization of the metal-free state. The present results suggest that the investigation of the solution state coupled with that of the crystal state can provide major insights into SOD1 pathway toward oligomerization in relation to fALS.

Reviews - 3ecv mentioned but not cited (1)

  1. Structural Properties and Interaction Partners of Familial ALS-Associated SOD1 Mutants. Huai J, Zhang Z. Front Neurol 10 527 (2019)

Articles - 3ecv mentioned but not cited (2)

  1. Structure and function of the Zika virus full-length NS5 protein. Zhao B, Yi G, Du F, Chuang YC, Vaughan RC, Sankaran B, Kao CC, Li P. Nat Commun 8 14762 (2017)
  2. Structural and dynamic aspects related to oligomerization of apo SOD1 and its mutants. Banci L, Bertini I, Boca M, Calderone V, Cantini F, Girotto S, Vieru M. Proc Natl Acad Sci U S A 106 6980-6985 (2009)


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  1. Metal-free superoxide dismutase forms soluble oligomers under physiological conditions: a possible general mechanism for familial ALS.. Banci L, Bertini I, Durazo A, Girotto S, Gralla EB, Martinelli M, Valentine JS, Vieru M, Whitelegge JP Proc. Natl. Acad. Sci. U.S.A. 104 11263-11267 (2007)
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