7v53 | pdb_00007v53

Crystal structure of full-length phospholipase D from Pseudomonas aeruginosa PAO1

spinqualitylabelsall models 7v53, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7v53 is a 1 chain structure with sequence from Pseudomonas aeruginosa PAO1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q9HYC2_PSEAE Publication Abstract from PubMed 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. Structural insights into PA3488-mediated inactivation of Pseudomonas aeruginosa PldA.,Yang X, Li Z, Zhao L, She Z, Gao Z, Sui SF, Dong Y, Li Y Nat Commun. 2022 Oct 10;13(1):5979. doi: 10.1038/s41467-022-33690-2. PMID:36216841 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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