5dir

membrane protein at 2.8 Angstroms

spinqualitylabelsall models 5dir, resolution 2.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5dir is a 8 chain structure with sequence from Pseudomonas aeruginosa PAO1 and Synthetic construct. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.8Å Ligands: 5BV, ALO, IIL, MLE, OLC Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function LSPA_PSEAE This protein specifically catalyzes the removal of signal peptides from prolipoproteins. Publication Abstract from PubMed With functions that range from cell envelope structure to signal transduction and transport, lipoproteins constitute 2 to 3% of bacterial genomes and play critical roles in bacterial physiology, pathogenicity, and antibiotic resistance. Lipoproteins are synthesized with a signal peptide securing them to the cytoplasmic membrane with the lipoprotein domain in the periplasm or outside the cell. Posttranslational processing requires a signal peptidase II (LspA) that removes the signal peptide. Here, we report the crystal structure of LspA from Pseudomonas aeruginosa complexed with the antimicrobial globomycin at 2.8 angstrom resolution. Mutagenesis studies identify LspA as an aspartyl peptidase. In an example of molecular mimicry, globomycin appears to inhibit by acting as a noncleavable peptide that sterically blocks the active site. This structure should inform rational antibiotic drug discovery. Structural basis of lipoprotein signal peptidase II action and inhibition by the antibiotic globomycin.,Vogeley L, El Arnaout T, Bailey J, Stansfeld PJ, Boland C, Caffrey M Science. 2016 Feb 19;351(6275):876-80. doi: 10.1126/science.aad3747. PMID:26912896 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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