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

Research output: Contribution to journalArticleResearchpeer-review

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.β-Aminopeptidases are enzymes with the unique ability to hydrolyze N-terminal β-amino acids from synthetic β-peptides. Here, the crystal structure of a β-aminopeptidase isolated from a Burkholderia sp., BcA5-BapA, is reported. The BcA5-BapA structure shows a tetrameric arrangement, with each monomer adopting a four-layered αββα fold. Comparison with three characterized β-aminopeptidases shows that variation in the substrate-binding pockets may provide the basis for substrate specificity.

Original languageEnglish
Pages (from-to)386-392
Number of pages7
JournalActa Crystallographica. Section F: Structural Biology Communications
VolumeF73
Issue number7
DOIs
Publication statusPublished - 1 Jul 2017

Keywords

  • BcA5-BapA
  • Burkholderia sp
  • crystallization
  • Ntn hydrolases
  • β-amino acids
  • β-aminopeptidases

Cite this

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title = "Crystal structure of a β-aminopeptidase from an Australian Burkholderia sp.",
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 {\AA} 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.β-Aminopeptidases are enzymes with the unique ability to hydrolyze N-terminal β-amino acids from synthetic β-peptides. Here, the crystal structure of a β-aminopeptidase isolated from a Burkholderia sp., BcA5-BapA, is reported. The BcA5-BapA structure shows a tetrameric arrangement, with each monomer adopting a four-layered αββα fold. Comparison with three characterized β-aminopeptidases shows that variation in the substrate-binding pockets may provide the basis for substrate specificity.",
keywords = "BcA5-BapA, Burkholderia sp, crystallization, Ntn hydrolases, β-amino acids, β-aminopeptidases",
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Crystal structure of a β-aminopeptidase from an Australian Burkholderia sp. / John-White, Marietta; Dumsday, Geoff J.; Johanesen, Priscilla; Lyras, Dena; Drinkwater, Nyssa; McGowan, Sheena.

In: Acta Crystallographica. Section F: Structural Biology Communications, Vol. F73, No. 7, 01.07.2017, p. 386-392.

Research output: Contribution to journalArticleResearchpeer-review

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AU - Dumsday, Geoff J.

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