research communications
β-Aminopeptidases are a unique group of enzymes that have the unusual capability to hydrolyze N-terminal β-amino acids from synthetic β-peptides. β-Peptides can form secondary structures mimicking α-peptide-like structures that are resistant to degradation by most known proteases and peptidases. These characteristics of β-peptides give them great potential as peptidomimetics. Here, the X-ray crystal structure of BcA5-BapA, a β-aminopeptidase from a Gram-negative Burkholderia sp. that was isolated from activated sludge from a wastewater-treatment plant in Australia, is reported. The crystal structure of BcA5-BapA was determined to a resolution of 2.0 Å and showed a tetrameric assembly typical of the β-aminopeptidases. Each monomer consists of an α-subunit (residues 1–238) and a β-subunit (residues 239–367). Comparison of the structure of BcA5-BapA with those of other known β-aminopeptidases shows a highly conserved structure and suggests a similar proteolytic mechanism of action.
Keywords: BcA5-BapA; β-aminopeptidases; crystallization; Burkholderia sp.; β-amino acids; Ntn hydrolases.
Supporting information
Portable Document Format (PDF) file https://doi.org/10.1107/S2053230X17007737/hv5358sup1.pdf |
PDB reference: BcA5-bapA, 5tzb