Energetic coupling of an active site residue in penicillin-binding protein 2 from Neisseria gonorrhoeae with a resistance-associated conformational switch in the β3-β4 loop
NMR data, in combination with enzymatic assays using active variants confirmed differences in the active, apo states of these enzymes, and provided additional atomic detail regarding the importance of the P94 residue in saSrtA substrate recognition.
Erich G. Walkenhauer, Noah Cox-Tigre, M. Chaubey et al.· bioRxiv· 0 citations
Findings establish S118 and D159 as essential for core catalysis and structural integrity, with V120 and L158 modulating substrate-specific turnover and orientation.
Ajith Tejavath, Bayomi Biju, Aditya Prasad Panda et al.· ACS Infectious Diseases· 1 citation
Results support a model in which conserved hydrophobic active-site residues optimize the geometric and electrostatic environment required for efficient carbapenem deacylation and turnover, and provide mechanistic insight into OXA-48 catalysis that may be exploited to design inhibitors targeting the enzyme.
DorisMia Taylor, D. Ngango, Jia-Yi Fan et al.· ACS Infectious Diseases· 0 citations
ABSTRACT Escherichia coli with penicillin-binding protein 3 (PBP3) insertions appeared in the early 2000s and expanded during the 2010s. The YRIN and YRIK variants predominate globally, while other insertion types remain rare. These insertions frequently co-occur with carbapenemases (NDM-5 and OXA-181) and high-risk cl...
Johann D. D. Pitout, G. Peirano, Y. Matsumura et al.· Antimicrobial Agents and Che...· 0 citations
Non-typeable Haemophilus influenzae (NTHi) is an opportunistic extracellular pathogen associated with various respiratory diseases. To combat host antimicrobial peptides, NTHi has developed a specialized transporter named Sap (sensitivity to antimicrobial peptide). Within this transporter, the HiSapF component function...
Kalyan Ghosh, S. P. Kanaujia· International Journal of Bio...· 0 citations
Findings suggest that MSMEG_6194 act as a DD-carboxypeptidase and illustrate how a single amino acid change can alter catalytic preference, shedding light on the evolutionary transition from DD-carboxypeptidases to beta-lactamases in mycobacteria.
Aditya Prasad Panda, Debasmita Chatterjee, Anik Roy et al.· Current Microbiology· 0 citations
We use cookies to run the site and, with your consent, for analytics and to show ads.
See our Cookie Policy.