7bk8

X-ray crystal structure of Pseudomonas aeruginosa MagC

spinqualitylabelsall models 7bk8, resolution 1.74Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.74Å Ligands: PO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Bacterial alpha-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. MagC is a NplC/P60-like member of the alpha-2-macroglobulin Mag complex of Pseudomonas aeruginosa that interacts with peptidoglycan.,Zouhir S, Contreras-Martel C, Maragno Trindade D, Attree I, Dessen A, Macheboeuf P FEBS Lett. 2021 Jun 11. doi: 10.1002/1873-3468.14148. PMID:34115884 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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