Structural highlights
Publication Abstract from PubMedbeta-Aminopeptidases are a unique group of enzymes that have the unusual capability to hydrolyze N-terminal beta-amino acids from synthetic beta-peptides. beta-Peptides can form secondary structures mimicking alpha-peptide-like structures that are resistant to degradation by most known proteases and peptidases. These characteristics of beta-peptides give them great potential as peptidomimetics. Here, the X-ray crystal structure of BcA5-BapA, a beta-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 A and showed a tetrameric assembly typical of the beta-aminopeptidases. Each monomer consists of an alpha-subunit (residues 1-238) and a beta-subunit (residues 239-367). Comparison of the structure of BcA5-BapA with those of other known beta-aminopeptidases shows a highly conserved structure and suggests a similar proteolytic mechanism of action. Crystal structure of a beta-aminopeptidase from an Australian Burkholderia sp.,John-White M, Dumsday GJ, Johanesen P, Lyras D, Drinkwater N, McGowan S Acta Crystallogr F Struct Biol Commun. 2017 Jul 1;73(Pt 7):386-392. doi:, 10.1107/S2053230X17007737. Epub 2017 Jun 17. PMID:28695846[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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