5TZB
Burkholderia sp. beta-aminopeptidase
Summary for 5TZB
| Entry DOI | 10.2210/pdb5tzb/pdb |
| Descriptor | D-aminopeptidase, CALCIUM ION (3 entities in total) |
| Functional Keywords | beta-aminopeptidase, enzyme, burkholderia, ntn hydrolases, beta-amino acids, hydrolase |
| Biological source | Burkholderia sp. LK4 |
| Total number of polymer chains | 8 |
| Total formula weight | 320863.82 |
| Authors | McGowan, S.,Drinkwater, N.,John, M.,Dumsday, G. (deposition date: 2016-11-21, release date: 2017-07-12, Last modification date: 2023-10-04) |
| Primary citation | 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 Cited by 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: 28695846DOI: 10.1107/S2053230X17007737 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.977 Å) |
Structure validation
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