D
IPR001424

Superoxide dismutase, copper/zinc binding domain

InterPro entry
Short nameSOD_Cu_Zn_dom
Overlapping
homologous
superfamilies
 

Description

Superoxide dismutases (SODs) are ubiquitous metalloproteins that prevent damage by oxygen-mediated free radicals by catalysing the dismutation of superoxide into molecular oxygen and hydrogen peroxide
[4]
. Superoxide is a normal by-product of aerobic respiration and is produced by a number of reactions, including oxidative phosphorylation and photosynthesis. The dismutase enzymes have a very high catalytic efficiency due to the attraction of superoxide to the ions bound at the active site
[3, 2]
.

There are three forms of superoxide dismutase, depending on the metal cofactor: Cu/Zn (which binds both copper and zinc), Fe and Mn types. The Fe and Mn forms are similar in their primary, secondary and tertiary structures, but are distinct from the Cu/Zn form
[1]
. Prokaryotes and protists contain Mn, Fe or both types, while most eukaryotic organisms utilise the Cu/Zn type.

Defects in the human SOD1 gene causes familial amyotrophic lateral sclerosis (Lou Gehrig's disease). Cytoplasmic and periplasmic SODs exist as dimers, whereas chloroplastic and extracellular enzymes exist as tetramers. Structural analysis supports the notion of independent functional evolution in prokaryotes (P-class) and eukaryotes (E-class)
[5, 11, 12, 6, 7, 8, 9, 10]
.

References

1.Characterization of iron superoxide dismutase cDNAs from plants obtained by genetic complementation in Escherichia coli. Van Camp W, Bowler C, Villarroel R, Tsang EW, Van Montagu M, Inze D. Proc. Natl. Acad. Sci. U.S.A. 87, 9903-7, (1990). View articlePMID: 2263641

2.Primary structure of porcine Cu,Zn superoxide dismutase. Schinina ME, Barra D, Simmaco M, Bossa F, Rotilio G. FEBS Lett. 186, 267-70, (1985). View articlePMID: 3891411

3.Atomic structures of wild-type and thermostable mutant recombinant human Cu,Zn superoxide dismutase. Parge HE, Hallewell RA, Tainer JA. Proc. Natl. Acad. Sci. U.S.A. 89, 6109-13, (1992). View articlePMID: 1463506

4.Primary structure from amino acid and cDNA sequences of two Cu,Zn superoxide dismutase variants from Xenopus laevis. Schinina ME, Barra D, Bossa F, Calabrese L, Montesano L, Carri MT, Mariottini P, Amaldi F, Rotilio G. Arch. Biochem. Biophys. 272, 507-15, (1989). View articlePMID: 2751312

5.Conserved patterns in the Cu,Zn superoxide dismutase family. Bordo D, Djinovic K, Bolognesi M. J. Mol. Biol. 238, 366-86, (1994). View articlePMID: 8176730

6.A structure-based mechanism for copper-zinc superoxide dismutase. Hart PJ, Balbirnie MM, Ogihara NL, Nersissian AM, Weiss MS, Valentine JS, Eisenberg D. Biochemistry 38, 2167-78, (1999). View articlePMID: 10026301

7.Unusual trigonal-planar copper configuration revealed in the atomic structure of yeast copper-zinc superoxide dismutase. Ogihara NL, Parge HE, Hart PJ, Weiss MS, Goto JJ, Crane BR, Tsang J, Slater K, Roe JA, Valentine JS, Eisenberg D, Tainer JA. Biochemistry 35, 2316-21, (1996). View articlePMID: 8652572

8.The solution structure of reduced dimeric copper zinc superoxide dismutase. The structural effects of dimerization. Banci L, Bertini I, Cramaro F, Del Conte R, Viezzoli MS. Eur. J. Biochem. 269, 1905-15, (2002). View articlePMID: 11952792

9.Backbone dynamics of human Cu,Zn superoxide dismutase and of its monomeric F50E/G51E/E133Q mutant: the influence of dimerization on mobility and function. Banci L, Bertini I, Cramaro F, Del Conte R, Rosato A, Viezzoli MS. Biochemistry 39, 9108-18, (2000). View articlePMID: 10924104

10.Aspects of the structure, function, and applications of superoxide dismutase. Bannister JV, Bannister WH, Rotilio G. CRC Crit. Rev. Biochem. 22, 111-80, (1987). PMID: 3315461

11.Novel dimeric interface and electrostatic recognition in bacterial Cu,Zn superoxide dismutase. Bourne Y, Redford SM, Steinman HM, Lepock JR, Tainer JA, Getzoff ED. Proc. Natl. Acad. Sci. U.S.A. 93, 12774-9, (1996). View articlePMID: 8917495

12.Cu,Zn superoxide dismutase structure from a microbial pathogen establishes a class with a conserved dimer interface. Forest KT, Langford PR, Kroll JS, Getzoff ED. J. Mol. Biol. 296, 145-53, (2000). View articlePMID: 10656823

GO terms

cellular component

  • None

Cross References

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