5TZB

Burkholderia sp. beta-aminopeptidase

5TZB の概要

• エントリーDOI: 10.2210/pdb5tzb/pdb
• 分子名称: D-aminopeptidase, CALCIUM ION (3 entities in total)
• 機能のキーワード: beta-aminopeptidase, enzyme, burkholderia, ntn hydrolases, beta-amino acids, hydrolase
• 由来する生物種: Burkholderia sp. LK4
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 320863.82

構造登録者

McGowan, S.,Drinkwater, N.,John, M.,Dumsday, G. (登録日: 2016-11-21, 公開日: 2017-07-12, 最終更新日: 2023-10-04)

主引用文献

John-White, M.,Dumsday, G.J.,Johanesen, P.,Lyras, D.,Drinkwater, N.,McGowan, S.
Crystal structure of a beta-aminopeptidase from an Australian Burkholderia sp.
Acta Crystallogr F Struct Biol Commun, 73:386-392, 2017

PubMed 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.

PubMed: 28695846
DOI: 10.1107/S2053230X17007737

実験手法

X-RAY DIFFRACTION (1.977 Å)