InterPro domain: IPR011254

Prismane (hybrid-cluster) proteins are present in a wide range of bacteria and archaea, and are characterised by their two Fe/S centres: a [4Fe-4S] cubane cluster, and a hybrid [4Fe-2S-2O] cluster [ 1 ]. Prismane proteins contain four domains: two spectrin repeat-like 3-helical bundle domains, and two alpha/beta domains with Rossmann-fold topology. Several proteins are structurally related to Prismane, including Ni-containing carbon monoxide dehydrogenase (CODH) (lack one of the N-terminal 3-helical bundle domains), the alpha and beta subunits of bifunctional CODH, and the alpha and beta subunits of acetyl-CoA synthetase.

This superfamily represents the spectrin repeat-like 3-helical bundle domains, as well as the two alpha/beta domains with Rossmann-fold topology.

1. The hybrid-cluster protein ('prismane protein') from Escherichia coli. Characterization of the hybrid-cluster protein, redox properties of the [2Fe-2S] and [4Fe-2S-2O] clusters and identification of an associated NADH oxidoreductase containing FAD and [2Fe-2S]. Eur. J. Biochem. 267, 666-76