Abstract
The bacterial cell wall is essential for survival, and proteins that participate in its biosynthesis have been the targets of antibiotic development efforts for decades. The biosynthesis of its main component, the peptidoglycan, involves the coordinated action of proteins that are involved in multi-member complexes which are essential for cell division (the “divisome”) and/or cell wall elongation (the “elongasome”), in the case of rod-shaped cells. Our knowledge regarding these interactions has greatly benefitted from the visualization of different aspects of the bacterial cell wall and its cytoskeleton by cryoelectron microscopy and tomography, as well as genetic and biochemical screens that have complemented information from high resolution crystal structures of protein complexes involved in divisome or elongasome formation. This review summarizes structural and functional aspects of protein complexes involved in the cytoplasmic and membrane-related steps of peptidoglycan biosynthesis, with a particular focus on protein-protein interactions whereby disruption could lead to the development of novel antibacterial strategies.
Highlights
Peptidoglycan (PG) is a key component of the bacterial cell wall, and plays an important role in bacterial shape, as well as division and elongation processes
In rod-shaped bacteria, the orchestration of cellular morphogenesis occurs in two phases: cell division, which generates two daughter cells, and elongation, where cellular growth occurs along the longitudinal axis of the cell
The sheer complexity of the bacterial cell wall biosynthetic pathway has created significant challenges for the characterization of proteins that are involved in the different aspects of the process
Summary
Peptidoglycan (PG) is a key component of the bacterial cell wall, and plays an important role in bacterial shape, as well as division and elongation processes. The integral membrane protein catalyzes cytoplasmic step involves the link between Lipid I and a GlcNAc molecule by the membrane-associated the transfer of the phospho-MurNAc-pentapeptide motif of UDP-MurNAc-pentapeptide to a lipid enzyme MurG, generating Lipid II [9,10], which is eventually translocated to the periplasmic side of carrier, undecaprenyl phosphate, to form Lipid I [8,9]. GlcNAc-MurNAc-pentapeptide into the PG layer through glycosylation and transpeptidation as being members of distinct protein complexes Anchors the UDP-NAM-pentapeptide unit to inner membrane of the final peptidoglycan building block PDB codes of molecules depicted here: MurA (1NAW); MurB (1MBT); MurC (1J6U); MurD (4BUC); MurE (4BUB); MurF (3ZL8); MurG (1F0K); MraY (4J72)
Sign-in/Register to view highlights & summary Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
