biostudies-literatureWang SMinistry of Science and Technology, TaiwanMinistry of Science and Technology, Taiwan (Ministry of Science and Technology of Taiwan)5461https://www.ebi.ac.uk/biostudies/studies/S-EPMC11211486biostudies-literatureUnknown15(1)Peptidoglycan (PG) sacculi surround the cytoplasmic membrane, maintaining cell integrity by withstanding internal turgor pressure. During cell growth, PG endopeptidases cleave the crosslinks of the fully closed sacculi, allowing for the incorporation of new glycan strands and expansion of the peptidoglycan mesh. Outer-membrane-anchored NlpI associates with hydrolases and synthases near PG synthesis complexes, facilitating spatially close PG hydrolysis. Here, we present the structure of adaptor NlpI in complex with the endopeptidase MepS, revealing atomic details of how NlpI recruits multiple MepS molecules and subsequently influences PG expansion. NlpI binding elicits a disorder-to-order transition in the intrinsically disordered N-terminal of MepS, concomitantly promoting the dimerizationNature communicationsStructural basis for recruitment of peptidoglycan endopeptidase MepS by lipoprotein NlpI.PMC11211486109-2113-M-002-018112-2113-M-002-016Wang SWChang YYYeh YQLin TSWang STzeng SRHuang CHTseng HCFan YSHuang SJChang CIJeng USfalseStructural basis for recruitment of peptidoglycan endopeptidase MepS by lipoprotein NlpI.Peptidoglycan (PG) sacculi surround the cytoplasmic membrane, maintaining cell integrity by withstanding internal turgor pressure. During cell growth, PG endopeptidases cleave the crosslinks of the fully closed sacculi, allowing for the incorporation of new glycan strands and expansion of the peptidoglycan mesh. Outer-membrane-anchored NlpI associates with hydrolases and synthases near PG synthesis complexes, facilitating spatially close PG hydrolysis. Here, we present the structure of adaptor NlpI in complex with the endopeptidase MepS, revealing atomic details of how NlpI recruits multiple MepS molecules and subsequently influences PG expansion. NlpI binding elicits a disorder-to-order transition in the intrinsically disordered N-terminal of MepS, concomitantly promoting the dimerization2024-01-01T00:00:00Z2024 Jun2026-05-29T14:29:36.907Z2026-04-08T05:05:01.333ZS-EPMC112114863893743310.1038/s41467-024-49552-y