6yn0

Structure of E. coli PBP1b with a FtsN peptide activating transglycosylase activityStructure of E. coli PBP1b with a FtsN peptide activating transglycosylase activity

Structural highlights 6yn0 is a 2 chain structure with sequence from Escherichia coli K-12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.4Å Ligands: Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function FTSN_ECOLI Essential cell division protein. May play a role in the assembly or stability of the septation machinery. May interact with FtsA, PBP3 and FtsQ. Publication Abstract from PubMed 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 Escherichia coli, septal PG synthesis and cell constriction rely on the accumulation of FtsN at the division site. Interestingly, a short sequence of FtsN (L75 to Q93, known as (E)FtsN) was shown to be essential and sufficient for its functioning in vivo, but what exactly this sequence is doing remained unknown. Here, we show that (E)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 (E)FtsN, which demonstrates (E)FtsN binds at the junction between the GTase and UB2H domains of PBP1b. Interestingly, mutations to two residues (R141A/R397A) within the (E)FtsN binding pocket reduced the activation of PBP1b by FtsN but not by the lipoprotein LpoB. This mutant was unable to rescue DeltaponB-ponAts strain, that lack PBP1b and has a thermosensitive PBP1a, at nonpermissive temperature and induced a mild cell chaining phenotype and cell lysis. Altogether, the results show that (E)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. The bacterial cell division protein fragment (E)FtsN binds to and activates the major peptidoglycan synthase PBP1b.,Boes A, Kerff F, Herman R, Touze T, Breukink E, Terrak M J Biol Chem. 2020 Oct 27. pii: RA120.015951. doi: 10.1074/jbc.RA120.015951. PMID:33109614 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Cell division protein 3D structures Penicillin-binding protein 3D structures

spinqualitylabelsall models 6yn0, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image