5WQL

Structure of a PDZ-protease bound to a substrate-binding adaptor

5WQL の概要

• エントリーDOI: 10.2210/pdb5wql/pdb
• 分子名称: Lipoprotein NlpI, Tail-specific protease, ALA-ALA-ALA-ALA-ALA-ALA, ... (6 entities in total)
• 機能のキーワード: prc, nlpi, protein degradation, peptidoglycan, protein binding-signaling protein-hydrolase-peptide complex, protein binding/signaling protein/hydrolase/peptide
• 由来する生物種: Escherichia coli K-12; 詳細
• 細胞内の位置: Cell membrane; Lipid-anchor: P0AFB1; Cell inner membrane; Peripheral membrane protein; Periplasmic side: P23865
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 218800.37

構造登録者

Su, M.Y.,Chang, C.I. (登録日: 2016-11-27, 公開日: 2017-11-22, 最終更新日: 2023-11-08)

主引用文献

Su, M.Y.,Som, N.,Wu, C.Y.,Su, S.C.,Kuo, Y.T.,Ke, L.C.,Ho, M.R.,Tzeng, S.R.,Teng, C.H.,Mengin-Lecreulx, D.,Reddy, M.,Chang, C.I.
Structural basis of adaptor-mediated protein degradation by the tail-specific PDZ-protease Prc
Nat Commun, 8:1516-1516, 2017

PubMed Abstract: Peptidoglycan (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.

PubMed: 29138488
DOI: 10.1038/s41467-017-01697-9

実験手法

X-RAY DIFFRACTION (2.3 Å)