{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD064453/QEX02_VR_251113_SN_TOC_XL_B7_095.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD064453/QEX02_VR_251113_SN_TOC_XL_B2_080.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD064453/QEX02_VR_251113_SN_TOC_XL_B4_086.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD064453/QEX03_VR_250228_SN_1_XL_TOC_1h_337.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD064453/QEX02_VR_251113_SN_TOC_XL_B8_098.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD064453/QEX03_MF_250228_SN_1_XL_TOC_2h_347.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD064453/QEX02_VR_251113_SN_TOC_XL_B3_083.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD064453/QEX02_VR_251113_SN_TOC_XL_B6_092.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD064453/QEX03_MF_250228_SN_2_XL_TOC_2h_351.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD064453/QEX03_VR_250228_SN_2_XL_TOC_1h_341.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD064453/QEX02_VR_251114_SN_TOC_XL_B1_077.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD064453/QEX02_VR_251113_SN_TOC_XL_B5_089.raw"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD064453/MetaMorpheus_Results.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD064453/pLINK_Results.zip"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["marjorie.fournier@bioch.ox.ac.uk"],"submitter":["Vaishnavi Ravikumar"],"technology_type":["Mass Spectrometry","Chemical cross-linking coupled with mass spectrometry proteomics"],"software":[""],"submitter_keywords":[""],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD064453"],"sample_protocol":["The HA-purified TOC complex was crosslinked with 3 mM bis(sulfosuccinimidyl)suberate (BS3) (Thermo Scientific) at room temperature for 3 h. The reaction was terminated by adding 50 mM Tris. Detergent (DDM) was removed by using HiPPR detergent removal resin (Thermo Scientific) prior to the preparation of the samples for mass spectrometry (MS). The crosslinked samples were denatured in 4 M urea (100 mM ammonium bicarbonate, pH 7.8) for 10 min, before cysteine reduction with 10 mM Tris(2-carboxyethyl)phosphine (TCEP) for 30 min at room temperature, and alkylation with 50 mM 2-chloroacetamide for 30 min at room temperature in the dark. Next, the samples were pre-digested with endoproteinase LysC (Wako) (1:100 µg enzyme:protein ratio) at 37 °C for 2 h, 700 rpm and then further digested with trypsin (Promega) (1:40 µg enzyme:protein ratio) for 16 h. The digested peptides were loaded onto C18 stage tips, pre-activated with 100 % acetonitrile and 0.1 % trifluoroacetic acid. Centrifugation was carried out at 4000 rpm at room temperature. Subsequently, peptides were washed with 0.1 % trifluoroacetic acid and eluted in 50 % acetonitrile / 0.1 % trifluoroacetic acid. Eluted peptides were dried in a speed-vac. Dried peptides were resuspended into 5 % acetonitrile / 5 % formic acid before LC-MS/MS analysis. Peptides were separated by nano liquid chromatography (Thermo Scientific Ultimate RSLC 3000) coupled in line to a QExactive mass spectrometer equipped with an Easy-Spray source (Thermo Fisher Scientific). Peptides were trapped onto a C18 PepMac100 precolumn (300 µm i.d. x 5 mm, 100 Å, Thermo Fisher Scientific) using Solvent A (0.1 % Formic acid, HPLC grade water). The peptides were further separated onto an Easy-Spray RSLC C18 column (75 µm i.d., 50 cm length, Thermo Fisher Scientific) using a 60 and 120 minute linear gradient (15 % to 35 % solvent B (0.1 % formic acid in acetonitrile)) at a flow rate 200 nL/min. The raw data were acquired on the mass spectrometer in a data-dependent acquisition mode (DDA). Full-scan MS spectra were acquired in the Orbitrap (Scan range 350-1500 m/z, resolution 70,000; AGC target, 3e6, maximum injection time, 50 ms. The 10 (60 min gradient) and 20 (120 min gradient) most intense peaks were selected for higher-energy collision dissociation (HCD) fragmentation at 30 % of normalized collision energy. HCD spectra were acquired in the Orbitrap at resolution 17,500, AGC target 5e4, maximum injection time of 120 ms with fixed mass at 180 m/z. Charge exclusion was selected for unassigned and 1+ ions. The dynamic exclusion was set to 20 s and 40 s for 60 min gradients and 120 min gradient respectively."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["Acquired tandem mass (MS/MS) spectra were searched using pLINK3 (ref) and MetaMorpheus 1.0.9 (ref), against an Arabidopsis thaliana database (Proteome ID UP000006548) downloaded from UniProt (2024_03_14), containing 18,300 protein entries and the tagged Toc75 protein sequence. In addition, 292 contaminant sequences were added to the database while processing with pLINK3. The default contaminant database of MetaMorpheus was used. The following variable modifications were set - Oxidation (M), Acetylation (N-ter). Carbamidomethylation was set as a fixed modification. Data was filtered at FDR below 5 %. Trypsin was set as the endoprotease. All identified crosslinked spectra were manually inspected and validated."],"omics_type":["Proteomics"],"labhead":["Marjorie Fournier"],"instrument_platform":[""],"labhead_affiliation":["Deaprtment of Biochemistry, University of Oxford"],"submission_type":["PARTIAL"],"species":["Arabidopsis Thaliana (mouse-ear Cress)"],"submitter_mail":["vaishnavi.ravikumar@gmail.com"],"publication":["Not available"],"submitter_affiliation":["Dept. of Biochemistry, University of Oxford"],"submitter_country":["United Kingdom"],"additional_accession":[]},"is_claimable":false,"name":"Assembly of two functionally-distinct protein import complexes in the outer membrane of plant chloroplasts (crosslinking data)","description":"The TOC protein translocon delivers thousands of nucleus-encoded proteins to chloroplasts and to related non-photosynthetic plastids. It comprises the β-barrel channel, Toc75, and multiple isoforms of receptor GTPases, Toc33 and Toc159. However, exactly how TOC complexes are assembled in different plastid types, is not known. Here, we present detailed characterization of two distinct TOC complexes, TOC-P and TOC-N, from photosynthetic chloroplasts and non-photosynthetic plastids, respectively. The assembled complexes are distinguished by having different sets of receptors, but both possess Toc75 which we identify as a central hub in TOC biogenesis: assembly is driven by TOC75 expression, with the Toc33and Toc159 GTPases being added sequentially thereafter. Integrative structural analysis revealed a modular architecture for TOC-P comprising a cytosolic GTPase receptor module linked flexibly to a membrane β-barrel channel module. TOC-N has a similar overall architecture, albeit with some clear differences that likely account for observed functional differences related to client 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