12006af28c825c060fa093dc942a93c9 pmc_32513917.pdf 2e5bbf868f0e4705751025498512ac0673bd6976 pmc_32513917.pdf 4b9a0d3f1965ac4e93d7b345453b77b86a4c018c5cb664f38b4d2753d55d6449 pmc_32513917.pdf Title: Structure and mechanism of the Nap adhesion complex from the human pathogen Mycoplasma genitalium Subject: Nature Communications, doi:10.1038/s41467-020-16511-2 Keywords: Author: David Aparicio Creator: Springer Producer: iText® 5.3.5 ©2000-2012 1T3XT BVBA (SPRINGER SBM; licensed version) CreationDate: Wed May 27 17:23:29 2020 CEST ModDate: Tue Jun 2 14:03:48 2020 CEST Custom Metadata: yes Metadata Stream: yes Tagged: no UserProperties: no Suspects: no Form: AcroForm JavaScript: no Pages: 10 Encrypted: no Page size: 595.276 x 782.362 pts Page rot: 0 File size: 3714503 bytes Optimized: no PDF version: 1.4 name type encoding emb sub uni object ID ------------------------------------ ----------------- ---------------- --- --- --- --------- FONBPB+AdvOTea1a7398 Type 1C WinAnsi yes yes no 50 0 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Well-Formed and valid SignatureMatches: PDF-hul MIMEtype: application/pdf PDFMetadata: Objects: 663 FreeObjects: 1 IncrementalUpdates: 0 DocumentCatalog: PageLayout: SinglePage PageMode: UseOutlines Language: EN Outlines: Item: Title: Structure and mechanism of the Nap adhesion complex from the human pathogen Mycoplasma genitalium Destination: title_link Children: Item: Title: Results Destination: A1 Children: Item: Title: Crystal structure of P140 and in complex with P110N Destination: B1 Item: Title: Structural similarities of P140 and P110 Destination: B2 Item: Title: Binding site analysis of the Nap Destination: B3 Item: Title: Single-particle cryo-EM of the P140–nobreakP110 extracellular region Destination: B4 Item: Title: Motility analysis of mutants Destination: B5 Item: Title: Single-particle analysis of the Nap Destination: B6 Item: Title: Cryo-electron tomography of the in’situ Nap Destination: B7 Item: Title: Discussion Destination: A2 Item: Title: Methods Destination: A3 Children: Item: Title: Cloning, expression, and purification of P110N, P140, and P110 Destination: B8 Item: Title: Preparation of P140–nobreakP110 and P140–nobreakP110N complexes and SEC-MALS analysis Destination: B9 Item: Title: Preparation of purified Nap complexes Destination: B10 Item: Title: Crystallization of P140 alone and the P140–nobreakP110N complex Destination: B11 Item: Title: X-ray data collection and structure determination Destination: B12 Item: Title: Cryo-ET and sub-tomogram averaging Destination: B13 Item: Title: Single-particle cryo-EM Destination: B14 Item: Title: Single-particle cryo-EM image processing Destination: B15 Item: Title: Surface plasmon resonance Destination: B16 Item: Title: Strains, culture conditions, and primers Destination: B17 Item: Title: DNA manipulation and mutant construction Destination: B18 Item: Title: Transformation and screening Destination: B19 Item: Title: Sequencing reactions Destination: B20 Item: Title: SDS-PAGE Destination: B21 Item: Title: Quantitative hemadsorption assay Destination: B22 Item: Title: Time-lapse microcinematography Destination: B23 Item: Title: Reporting summary Destination: B24 Item: Title: Data availability Destination: M1 Item: Title: Code availability Destination: M2 Item: Title: References Destination: A4 Item: Title: Acknowledgements Destination: A5 Item: Title: Author contributions Destination: A6 Item: Title: Competing interests Destination: A7 Item: Title: Additional information Destination: M3 Info: Title: Structure and mechanism of the Nap adhesion complex from the human pathogen Mycoplasma genitalium Author: David Aparicio Subject: Nature Communications, doi:10.1038/s41467-020-16511-2 Keywords: Creator: Springer Producer: iText® 5.3.5 ©2000-2012 1T3XT BVBA (SPRINGER SBM; licensed version) CreationDate: Wed May 27 17:53:29 CEST 2020 ModDate: Tue Jun 02 14:03:48 CEST 2020 ID: 0xd9d17de6d69611b2e246eae15da5f3b0, 0x6974bd2ae1a7d4589e0f0f702c48818e Filters: FilterPipeline: FlateDecode 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FontName: FONPOH+AdvOT7d6df7ab.I Flags: Serif, Nonsymbolic FontBBox: -135, -250, 1000, 854 FontFile3: true Encoding: WinAnsiEncoding Font: BaseFont: FONPOI+AdvOT1ef757c0+20 FontSubset: true FirstChar: 146 LastChar: 151 FontDescriptor: FontName: FONPOI+AdvOT1ef757c0+20 Flags: Nonsymbolic FontBBox: -135, -187, 1010, 833 FontFile3: true Encoding: WinAnsiEncoding Font: BaseFont: FOOMGA+Helvetica FontSubset: true FirstChar: 32 LastChar: 197 FontDescriptor: FontName: FOOMGA+Helvetica Flags: Nonsymbolic FontBBox: -166, -225, 1000, 931 FontFile3: true Encoding: WinAnsiEncoding Font: BaseFont: FOOMIA+Helvetica-Bold FontSubset: true FirstChar: 97 LastChar: 99 FontDescriptor: FontName: FOOMIA+Helvetica-Bold Flags: Nonsymbolic, ForceBold FontBBox: -170, -228, 1003, 962 FontFile3: true Encoding: WinAnsiEncoding XMP: application/pdf doi:10.1038/s41467-020-16511-2 Structure and mechanism of the Nap adhesion complex from the human pathogen Mycoplasma genitalium David Aparicio Margot P. Scheffer Marina Marcos-Silva David Vizarraga Lasse Sprankel Mercè Ratera Miriam S. Weber Anja Seybert Sergi Torres-Puig Luis Gonzalez-Gonzalez Julian Reitz Enrique Querol Jaume Piñol Oscar Q. Pich Ignacio Fita Achilleas S. Frangakis Springer US Nature Communications, doi:10.1038/s41467-020-16511-2 10.1038/s41467-020-16511-2 http://dx.doi.org/10.1038/s41467-020-16511-2 journal Nature Communications © 2020, The Author(s) 2041-1723 10.1038/s41467-020-16511-2 springer.com springerlink.com 2010-04-23 True 10.1038/s41467-020-16511-2 springer.com springerlink.com Springer 2020-06-02T14:03:48+02:00 2020-05-27T20:53:29+05:30 2020-06-02T14:03:48+02:00 True iText® 5.3.5 ©2000-2012 1T3XT BVBA (SPRINGER SBM; licensed version) VoR uuid:f13df00b-a2b2-4098-ad93-2846ca075cfc uuid:f6c3a8c5-a622-46f6-9d02-cd174719dcb2 default 1 converted uuid:9dd04d87-6f3d-4592-bbf2-a427eed6ee41 converted to PDF/A-2b pdfToolbox 2020-05-27T20:54:48+05:30 2 B Mercè Ratera http://orcid.org/0000-0001-5224-9172 Miriam S. 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