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MagC is a NplC/P60‐like member of the α‐2‐macroglobulin Mag complex of Pseudomonas aeruginosa that interacts with peptidoglycan
Author(s) -
Zouhir Samira,
ContrerasMartel Carlos,
Maragno Trindade Daniel,
Attrée Ina,
Dessen Andréa,
Macheboeuf Pauline
Publication year - 2021
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.14148
Subject(s) - peptidoglycan , macroglobulin , operon , pseudomonas aeruginosa , chemistry , ultracentrifuge , biochemistry , protease , gene , biology , bacteria , genetics , enzyme , escherichia coli
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.