Binding Site

Manganese/iron superoxide dismutase, binding site (IPR019833)

Short name: Mn/Fe_SOD_BS

Description

Superoxide dismutases (SODs) (EC:1.15.1.1) catalyse the conversion of superoxide radicals to molecular oxygen. Their function is to destroy the radicals that are normally produced within cells and are toxic to biological systems. Three evolutionarily distinct families of SODs are known, of which the Mn/Fe-binding family is one [PMID: 3315461, PMID: 3345848, PMID: 1556751]. This family includes both single metal-binding SODs and cambialistic SOD, which can bind either Mn or Fe. Fe/MnSODs are ubiquitous enzymes that are responsible for the majority of SOD activity in prokaryotes, fungi, blue-green algae and mitochondria. Fe/MnSODs are found as homodimers or homotetramers.

The structure of Fe/MnSODs can be divided into two domains, an alpha N-terminal domain and an alpha/beta C-terminal domain, connected by a loop. The structure of the N-terminal domain consists of a two helices in an antiparallel hairpin, with a left-handed twist [PMID: 9537987]. The structure of the C-terminal domain is of the alpha/beta type, and consists of a three-stranded antiparallel beta-sheet in the order 213, along with four helices in the arrangement alpha/beta(2)/alpha/beta/alpha(2) [PMID: 9931259].

Four residues conserved in the Fe/MnSODs are implicated in binding the metal ion. The pattern for this entry contains two of these conserved residues, an aspartate and a histidine.

GO terms

Biological Process

GO:0055114 oxidation-reduction process
GO:0006801 superoxide metabolic process

Molecular Function

GO:0046872 metal ion binding
GO:0004784 superoxide dismutase activity

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
PROSITE patterns