6YN0
Structure of E. coli PBP1b with a FtsN peptide activating transglycosylase activity
Summary for 6YN0
| Entry DOI | 10.2210/pdb6yn0/pdb |
| Descriptor | Penicillin-binding protein 1B, Cell division protein FtsN, MOENOMYCIN, ... (4 entities in total) |
| Functional Keywords | glycosyl transferase, penicillin binding protein, peptidoglycan synthesis, transferase |
| Biological source | Escherichia coli (strain K12) More |
| Total number of polymer chains | 2 |
| Total formula weight | 87320.74 |
| Authors | Kerff, F.,Terrak, M.,Boes, A.,Herman, H.,Charlier, P. (deposition date: 2020-04-10, release date: 2020-11-04, Last modification date: 2024-01-24) |
| Primary citation | Boes, A.,Kerff, F.,Herman, R.,Touze, T.,Breukink, E.,Terrak, M. The bacterial cell division protein fragment E FtsN binds to and activates the major peptidoglycan synthase PBP1b. J.Biol.Chem., 295:18256-18265, 2020 Cited by PubMed Abstract: Peptidoglycan (PG) is an essential constituent of the bacterial cell wall. During cell division, the machinery responsible for PG synthesis localizes mid-cell, at the septum, under the control of a multiprotein complex called the divisome. In , septal PG synthesis and cell constriction rely on the accumulation of FtsN at the division site. Interestingly, a short sequence of FtsN (Leu-Gln, known as FtsN) was shown to be essential and sufficient for its functioning , but what exactly this sequence is doing remained unknown. Here, we show that FtsN binds specifically to the major PG synthase PBP1b and is sufficient to stimulate its biosynthetic glycosyltransferase (GTase) activity. We also report the crystal structure of PBP1b in complex with FtsN, which demonstrates that FtsN binds at the junction between the GTase and UB2H domains of PBP1b. Interestingly, mutations to two residues (R141A/R397A) within the FtsN-binding pocket reduced the activation of PBP1b by FtsN but not by the lipoprotein LpoB. This mutant was unable to rescue the Δ- strain, which lacks PBP1b and has a thermosensitive PBP1a, at nonpermissive temperature and induced a mild cell-chaining phenotype and cell lysis. Altogether, the results show that FtsN interacts with PBP1b and that this interaction plays a role in the activation of its GTase activity by FtsN, which may contribute to the overall septal PG synthesis and regulation during cell division. PubMed: 33109614DOI: 10.1074/jbc.RA120.015951 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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