Induced conformational changes activate the peptidoglycan synthase PBP1B

• DOI: 10.1111/mmi.14082
• Publication Date: 2018-07-25T11:04:47Z
• Authors: Alexander J. F. Egan; Roberto Maya‐Mart...; Isabel Ayala; Catherine M. Boug...; Manuel Banzhaf; Eefjan Breukink; Waldemar Vollmer; Jean‐Pierre Simorre
• Keywords: Lipid II; Penicillin binding proteins; Inner membrane

Summary Bacteria surround their cytoplasmic membrane with an essential, stress‐bearing peptidoglycan (PG) layer consisting of glycan chains linked by short peptides into a mesh‐like structure. Growing and dividing cells expand PG using inner‐membrane anchored synthases, including Penicillin‐binding proteins (PBPs), which participate in dynamic protein complexes to facilitate cell wall growth. In Escherichia coli , presumably other Gram‐negative bacteria, growth the mainly single layered is regulated outer membrane‐anchored lipoproteins. The lipoprotein LpoB required activate PBP1B, major, bi‐functional synthase chain polymerising (glycosyltransferase) peptide cross‐linking (transpeptidase) activities. this work we show how binding regulatory UB2H domain PBP1B activates both Binding induces structural changes domain, transduce two catalytic domains distinct allosteric pathways. We also additional regulator protein, CpoB, able selectively modulate TPase activation without interfering GTase activation.