22c004e778001e8c2677b851a995f3de pmc_33837253.pdf 49e4896feff08b9a8556b24fc7e78b13b6d4b7d4 pmc_33837253.pdf bda7a91ba0ced0baa73af2f930efc3e51ad879d1e3777dc2865cda2277d523ac pmc_33837253.pdf Title: The Pseudomonas aeruginosa substrate-binding protein Ttg2D functions as a general glycerophospholipid transporter across the periplasm Subject: Communications Biology, doi:10.1038/s42003-021-01968-8 Keywords: Author: Daniel Yero Creator: Springer Producer: iText® 5.3.5 ©2000-2012 1T3XT BVBA (SPRINGER SBM; licensed version) CreationDate: Thu Apr 1 09:24:27 2021 CEST ModDate: Thu Apr 1 18:53:53 2021 CEST Custom Metadata: yes Metadata Stream: yes Tagged: no UserProperties: no Suspects: no Form: AcroForm JavaScript: no Pages: 16 Encrypted: no Page size: 595.276 x 782.362 pts Page rot: 0 File size: 3158071 bytes Optimized: no PDF version: 1.4 name type encoding emb sub uni object ID ------------------------------------ ----------------- ---------------- --- --- --- --------- HOPNFG+AdvOTf23bb480 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CEST Size: 3158071 Format: PDF Version: 1.4 Status: Well-Formed and valid SignatureMatches: PDF-hul MIMEtype: application/pdf PDFMetadata: Objects: 934 FreeObjects: 1 IncrementalUpdates: 0 DocumentCatalog: PageLayout: SinglePage PageMode: UseOutlines Language: EN Outlines: Item: Title: The Pseudomonas aeruginosa substrate-binding protein Ttg2D functions as a general glycerophospholipid transporter across the periplasm Destination: title_link Children: Item: Title: Results Destination: A1 Children: Item: Title: Ttg2DPae contains a large hydrophobic cavity that binds four acyl tails Destination: B1 Item: Title: The Ttg2D/MlaC fold: a new two-domain architecture and SBP structural cluster Destination: B2 Item: Title: Evolution of sequence and structural diversity of the MlaC family Destination: B3 Item: Title: Ttg2DPae binds two diacyl glycerophospholipids and cardiolipin, to our knowledge representing a novel phospholipid trafficking mechanism among Gram-negative bacteria Destination: B4 Item: Title: Ttg2DPae binds two diacyl glycerophospholipids or cardiolipin in the periplasm of P. aeruginosa Destination: B5 Item: Title: The Ttg2’system provides P. aeruginosa with a mechanism of resistance to membrane-damaging agents Destination: B6 Item: Title: The Ttg2’system is associated to P. aeruginosa’s intrinsic resistance to low antibiotic concentrations Destination: B7 Item: Title: Discussion Destination: A2 Item: Title: Methods Destination: A3 Children: Item: Title: Bacterial strains Destination: B8 Item: Title: Expression, purification, and preparation of Ttg2DPae protein variants Destination: B9 Item: Title: Ttg2DPae structure resolution Destination: B10 Item: Title: Delipidation of purified recombinant Ttg2DPae Destination: B11 Item: Title: Native MS analysis and identification of bound phospholipids Destination: B12 Item: Title: Cardiolipin binding to Ttg2DPae by native MS Destination: B13 Item: Title: Generation of markerless ttg2 mutants in MDR P. aeruginosa strains and complementations Destination: B14 Item: Title: OM permeabilization assay Destination: B15 Item: Title: Susceptibility to antibiotics and membrane-damaging agents Destination: B16 Item: Title: Biofilm formation Destination: B17 Item: Title: Bioinformatic analysis Destination: B18 Item: Title: Statistics and reproducibility Destination: B19 Item: Title: Reporting summary Destination: A4 Item: Title: Data availability Destination: M1 Item: Title: References Destination: A5 Item: Title: Acknowledgements Destination: A6 Item: Title: Author contributions Destination: A7 Item: Title: Competing interests Destination: A8 Item: Title: Additional information Destination: M3 Info: Title: The Pseudomonas aeruginosa substrate-binding protein Ttg2D functions as a general glycerophospholipid transporter across the periplasm Author: Daniel Yero Subject: Communications Biology, doi:10.1038/s42003-021-01968-8 Keywords: Creator: Springer Producer: iText® 5.3.5 ©2000-2012 1T3XT BVBA (SPRINGER SBM; 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