Browse the search results

Product release from human lysozyme is mediated by an intermediate state with transient weak interactions between the product and enzyme.

The protein CpoB regulates PBP1B activity in response to the Tol energy state, which facilitates feedback and synchronicity between envelope constriction processes during Gram-negative bacterial cell division.

Imaging experiments and simulations reveal that the biophysical mechanism for force generation needed to engulf a forespore is based on coordinated cell wall synthesis and degradation.

Polar elongating mycobacteria (Mycobacterium smegmatis) require specific cell wall chemistries, those catalyzed by targets of critical antibiotics, to maintain rod shape at aging sites of the bacillus.

Unlike other similar enzymes, the antimicrobial enzyme PlyC can interact with and translocate eukaryotic membranes, and then lyse and kill intracellular bacteria.

Uniform diameter and curvature of the outer membrane extensions and vesicles of Shewanella oneidensis are maintained by a bacterial Bin/Amphiphysin/Rvs (BAR) domain-like protein BdpA.

A wide range of bacterial species can switch into a cell wall-free state that does not require the FtsZ-based division machinery to proliferate.

Labeling with ¹³C and ¹⁵N in the absence of metabolic engineering enabled the exploration of peptidoglycan metabolism at a very fine level of detail based on kinetic characterization of isotopologues predicted to occur according to known recycling and biosynthesis pathways.

The N-terminal domain of Staphylococcus aureus GpsB, a scaffolding protein, forms an atypical asymmetric dimer and binds to the C-termini of FtsZ and PBP4, influencing the localization and regulation of both the Z-ring and cell wall synthesis.