7BK8
X-ray crystal structure of Pseudomonas aeruginosa MagC
Summary for 7BK8
| Entry DOI | 10.2210/pdb7bk8/pdb |
| Descriptor | MagC, PHOSPHATE ION (3 entities in total) |
| Functional Keywords | alpha-2-macroglobulin, peptidoglycan, nlpc/p60, endopeptidase, hydrolase, magc |
| Biological source | Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) |
| Total number of polymer chains | 1 |
| Total formula weight | 24123.24 |
| Authors | Zouhir, S.,Contreras-Martel, C.,Maragno Trindade, D.,Attree, I.,Dessen, A.,Macheboeuf, P. (deposition date: 2021-01-15, release date: 2021-07-21, Last modification date: 2024-06-19) |
| Primary citation | Zouhir, S.,Contreras-Martel, C.,Maragno Trindade, D.,Attree, I.,Dessen, A.,Macheboeuf, P. MagC is a NplC/P60-like member of the alpha-2-macroglobulin Mag complex of Pseudomonas aeruginosa that interacts with peptidoglycan. Febs Lett., 595:2034-2046, 2021 Cited by PubMed Abstract: 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. PubMed: 34115884DOI: 10.1002/1873-3468.14148 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.74 Å) |
Structure validation
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