MagC is a NplC/P60-like member of the α-2-macroglobulin Mag complex of Pseudomonas aeruginosa that interacts with peptidoglycan

FEBS Letters

article

Samira Zouhir¹  Carlos Contreras-Martel²  Daniel Maragno Trindade¹  Ina Attrée³  Andréa Dessen¹  Pauline Macheboeuf² 

[1] Brazilian Biosciences National Laboratory;CNRS, CEA, IBS, Université Grenoble Alpes;Unité de Biologie Cellulaire et Infection, CEA, INSERM, CNRS, Université Grenoble Alpes

关键词: α-2-macroglobulin;    NlpC/P60;    peptidoglycan hydrolase;   

DOI  :  10.1002/1873-3468.14148

来源: John Wiley & Sons Ltd.

【 摘 要 】

Bacterial α-2 macroglobulins (A2Ms) structurally resemble the large spectrum protease inhibitors of the eukaryotic immune system. In Pseudomonas aeruginosa , MagD acts as an A2M and is expressed within a six-gene operon encoding the MagA-F proteins. In this work, we employ isothermal calorimetry (ITC), analytical ultracentrifugation (AUC), and X-ray crystallography to investigate the function of MagC and show that MagC associates with the macroglobulin complex and with the peptidoglycan (PG). However, the catalytic residues of MagC display an inactive conformation that could suggest that it binds to PG but does not degrade it. We hypothesize that MagC could serve as an anchor between the MagD macroglobulin and the PG and could provide stabilization and/or regulation for the entire complex.

【 授权许可】

Unknown