Nearly all bacteria contain a peptidoglycan cell wall. The peptidoglycan precursor molecule is LipidII, containing the basic peptidoglycan building block attached to a lipid. Although the suitability of LipidII as an antibacterial target has long been recognized, progress on elucidating the role(s) of LipidII in bacterial cell biology has been slow. The focus of this review is on exciting new developments, both with respect to antibacterials targeting LipidII as well as the emerging role of LipidII in organizing the membrane and cell wall synthesis. It appears that on both sides of the membrane, LipidII plays crucial roles in organizing cytoskeletal proteins and peptidoglycan synthesis machineries. Finally, the recent discovery of no less than three different categories of LipidII flippases will be discussed.
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| http://dx.doi.org/10.1371/journal.ppat.1005213 | DOI Listing |
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Article Synopsis
- PknB is a crucial kinase for Mycobacterium tuberculosis, needed for its growth and survival both in lab settings and in living organisms.
- The study identifies key residues in the extracytoplasmic domain of PknB that are vital for binding to mDAP-containing LipidII, without which the bacterium cannot survive.
- Disruption of this binding leads to excessive phosphorylation of PknB and its substrates, resulting in cellular dysfunction and death, suggesting that ligand interaction is essential for proper PknB localization and activity regulation.
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