Sequence and Structure-Based Classification of PenA β-Lactamase from Burkholderia stabilis

The process of hydrolysis of the bond between amides of the four-membered β-lactam ring in Gram-negative bacteria is the key mechanism of resistance in β-lactamase enzymes. Because Burkholderia multivorans' PenA β-lactamase has been selected as a prototype sequence because it is associated with conditions such as cystic fibrosis and meningitis. In this study, the PenA β-lactamase sequence from Burkholderia multivorans was retrieved to demonstrate how multiple sequence alignment and phylogenetic analysis enable relationships between an initial sequence and its progeny. Additionally, this work demonstrates the close relationship between Burkholderia stabilis and Burkholderia cepacia in phylogenetic tree analysis. Consensus and sequence conservation have been noted in this work based on pattern analysis. Based on the crystal structure (PDB ID: 7DOO) of Burkholderia multivorans PenA β-lactamase Avibactam Complex, the active site residues in Burkholderia stabilis were shown using PDB files. The POCASA server was utilized for the active site investigation, and BIOVIA Discovery Studio 2019 was also used to show the results. Burkholderia stabilis is a major contributor to wound infection and produces non-invasive infections. PenA β-lactamase protein can be a target for antibiotic screening and inhibitor selection. Prominent active binding site residues of PenA Burkholderia stabilis, were shown to be interacted with the Avibactam based on molecular docking analysis.