Shwachman-Bodian-Diamond Syndrome Protein

The human Shwachman-Bodian-Diamond syndrome(SBDS) protein belongs to a very conserved family of proteins of unknown function; orthologues found in Archaea, as well as plants and other eukaryotes <ref>1<ref>. Evidence has been provided that the SBDS protein orthologues may play a role in RNA metabolism (1). Two groups of SBDS orthologues have been identified. Archaea, animals, and fungi have SBDS proteins with approximately 250 amino acid residues. However, SBDS protein of plants and protists has the C-terminal extensions around 100 to 250 amino acid residues (3). The resolution of the Archaeoglobulus fulgidus SBDS protein orthologue is at a resolution of 1.9 angstroms; showcasing a three domain architecture (4). The domain that is the most targeted for disease mutations is the N-terminal domain; containing a mixed alpha/beta fold. The central domain has a three-helical bundle, and the C-terminal domain has a ferredoxin-like fold (4).