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

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

Author information

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

PMID:
28695846
DOI:
10.1107/S2053230X17007737
[Indexed for MEDLINE]

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