7V53
Crystal structure of full-length phospholipase D from Pseudomonas aeruginosa PAO1
Summary for 7V53
| Entry DOI | 10.2210/pdb7v53/pdb |
| Descriptor | Phospholipase D (2 entities in total) |
| Functional Keywords | phospholipase d, toxin, hydrolase |
| 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 | 122478.06 |
| Authors | |
| Primary citation | Yang, X.,Li, Z.,Zhao, L.,She, Z.,Gao, Z.,Sui, S.F.,Dong, Y.,Li, Y. Structural insights into PA3488-mediated inactivation of Pseudomonas aeruginosa PldA. Nat Commun, 13:5979-5979, 2022 Cited by PubMed Abstract: PldA, a phospholipase D (PLD) effector, catalyzes hydrolysis of the phosphodiester bonds of glycerophospholipids-the main component of cell membranes-and assists the invasion of the opportunistic pathogen Pseudomonas aeruginosa. As a cognate immunity protein, PA3488 can inhibit the activity of PldA to avoid self-toxicity. However, the precise inhibitory mechanism remains elusive. We determine the crystal structures of full-length and truncated PldA and the cryogenic electron microscopy structure of the PldA-PA3488 complex. Structural analysis reveals that there are different intermediates of PldA between the "open" and "closed" states of the catalytic pocket, accompanied by significant conformational changes in the "lid" region and the peripheral helical domain. Through structure-based mutational analysis, we identify the key residues responsible for the enzymatic activity of PldA. Together, these data provide an insight into the molecular mechanisms of PldA invasion and its neutralization by PA3488, aiding future design of PLD-targeted inhibitors and drugs. PubMed: 36216841DOI: 10.1038/s41467-022-33690-2 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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