Crystal structure of a β-aminopeptidase from an Australian Burkholderia sp

Marietta John-White; Geoff J Dumsday; Priscilla Johanesen; Dena Lyras; Nyssa Drinkwater; Sheena McGowan

doi:10.1107/S2053230X17007737

Crystal structure of a β-aminopeptidase from an Australian Burkholderia sp

Acta Crystallogr F Struct Biol Commun. 2017 Jul 1;73(Pt 7):386-392. doi: 10.1107/S2053230X17007737. Epub 2017 Jun 17.

Authors

Marietta John-White¹, Geoff J Dumsday², Priscilla Johanesen¹, Dena Lyras¹, Nyssa Drinkwater¹, Sheena McGowan¹

Affiliations

¹ Biomedicine Discovery Institute, Department of Microbiology, Monash University, Clayton, Melbourne, VIC 3800, Australia.
² Manufacturing, CSIRO, Clayton, Melbourne, VIC 3800, Australia.

Abstract

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; Burkholderia sp.; Ntn hydrolases; crystallization; β-amino acids; β-aminopeptidases.

MeSH terms

Amino Acid Motifs
Aminopeptidases / chemistry*
Aminopeptidases / genetics
Aminopeptidases / metabolism
Bacterial Proteins / chemistry*
Bacterial Proteins / genetics
Bacterial Proteins / metabolism
Burkholderia / chemistry*
Burkholderia / enzymology
Burkholderia / isolation & purification
Catalytic Domain
Cloning, Molecular
Crystallography, X-Ray
Escherichia coli / genetics
Escherichia coli / metabolism
Gene Expression
Genetic Vectors / chemistry
Genetic Vectors / metabolism
Humans
Hydrophobic and Hydrophilic Interactions
Models, Molecular
Peptides / chemical synthesis
Peptides / chemistry*
Peptides / metabolism
Peptidomimetics / chemical synthesis
Peptidomimetics / chemistry*
Peptidomimetics / metabolism
Protein Binding
Protein Conformation, alpha-Helical
Protein Conformation, beta-Strand
Protein Interaction Domains and Motifs
Protein Multimerization
Proteolysis
Recombinant Fusion Proteins / chemistry
Recombinant Fusion Proteins / genetics
Recombinant Fusion Proteins / metabolism
Substrate Specificity
Wastewater / microbiology

Substances

Bacterial Proteins
Peptides
Peptidomimetics
Recombinant Fusion Proteins
Waste Water
Aminopeptidases
aminopeptidase B