9tyw

Crystal structure of L,D-transpeptidase PA2854 from Pseudomonas aeruginosa

spinqualitylabelsall models 9tyw, resolution 2.63Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9tyw is a 1 chain structure with sequence from Pseudomonas aeruginosa PA1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.63Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q9HZZ0_PSEAE Publication Abstract from PubMed Gram-negative bacteria have an elaborate envelope that is composed of an outer membrane, the cell wall, and the inner membrane, which collectively encase the cytoplasm. The outer membrane is covalently anchored to the peptidoglycan, the major constituent of the cell wall. We document that the gene product of PA2854 is the catalyst that performs this transformation between the cell wall and the outer-membrane lipoprotein OprI in live Pseudomonas aeruginosa. Furthermore, we reconstitute this reaction in vitro with the use of purified recombinant PA2854, OprI, and synthetic samples of the cell-wall peptidoglycan, in each case documenting the attachment of the side-chain epsilon-amino group of Lys83 of OprI to the peptide stem of the peptidoglycan. OprI forms a trimeric structure. The X-ray structure of the trimeric state of OprI was solved to 2.1 A resolution, which reveals it as an extended 82 A helix bundle. The X-ray structure of PA2854 was also solved at 2.63 A resolution. The enzyme is composed of three domains, which were documented to bind to the synthetic peptidoglycan and to OprI. The enzyme turns over both non-cross-linked and cross-linked peptidoglycan as its substrate. A model for the ternary assembly of the complex of PA2854-OprI-peptidoglycan is proposed based on the collective evidence. We document that anchoring of the outer membrane to the cell wall catalyzed by PA2854 does not appear to be a redundant reaction (product of more than one enzyme), in the absence of which the bacterium shows a weakened envelope, prone to disruption. Outer Membrane-Peptidoglycan Anchoring in Pseudomonas aeruginosa.,El-Araby AM, Perez de Jose U, Miguel-Ruano V, Lee M, Feltzer R, Avila-Cobian LF, Hesek D, Fisher JF, Hermoso JA, Mobashery S J Am Chem Soc. 2026 Jul 1;148(25):25740-25756. doi: 10.1021/jacs.6c03160. Epub , 2026 May 8. PMID:42100858 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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