5wql | pdb_00005wql
Structure of a PDZ-protease bound to a substrate-binding adaptor
Structural highlights
Function[NLPI_ECOLI] May be involved in cell division. May play a role in bacterial septation or regulation of cell wall degradation during cell division. Negatively controls the production of extracellular DNA (eDNA).[1] [2] [PRC_ECOLI] Involved in the cleavage of a C-terminal peptide of 11 residues from the precursor form of penicillin-binding protein 3 (PBP3). May be involved in protection of the bacterium from thermal and osmotic stresses. Publication Abstract from PubMedPeptidoglycan (PG) is a highly cross-linked, protective mesh-like sacculus that surrounds the bacterial cytoplasmic membrane. Expansion of PG is tightly coupled to growth of a bacterial cell and requires hydrolases to cleave the cross-links for insertion of nascent PG material. In Escherichia coli, a proteolytic system comprising the periplasmic PDZ-protease Prc and the lipoprotein adaptor NlpI contributes to PG enlargement by regulating cellular levels of MepS, a cross-link-specific hydrolase. Here, we demonstrate how NlpI binds Prc to facilitate the degradation of its substrate MepS by structural and mutational analyses. An NlpI homodimer binds two molecules of Prc and forms three-sided MepS-docking cradles using its tetratricopeptide repeats. Prc forms a monomeric bowl-shaped structure with a lid-like PDZ domain connected by a substrate-sensing hinge that recognizes the bound C terminus of the substrate. In summary, our study reveals mechanistic details of protein degradation by the PDZ-protease Prc bound to its cognate adaptor protein. Structural basis of adaptor-mediated protein degradation by the tail-specific PDZ-protease Prc.,Su MY, Som N, Wu CY, Su SC, Kuo YT, Ke LC, Ho MR, Tzeng SR, Teng CH, Mengin-Lecreulx D, Reddy M, Chang CI Nat Commun. 2017 Nov 15;8(1):1516. doi: 10.1038/s41467-017-01697-9. PMID:29138488[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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