{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD073177/checksum.txt"],"Csv":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD073177/xi_kinesin_total_XL_MS.csv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD073177/kinesin_mScarlet_separated_PeptidePairs_xiFDR2.3.10.csv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD073177/kinesin_mScarlet_separated_ppi_xiFDR2.3.10.csv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD073177/kinesin_mScarlet_separated_proteingroups_xiFDR2.3.10.csv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD073177/kinesin_mScarlet_separated_xiVIEW_xiFDR2.3.10.csv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD073177/kinesin_mScarlet_separated_NAPs_PeptidePairs_xiFDR2.3.10.csv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD073177/kinesin_mScarlet_separated_NAPs_PSM_xiFDR2.3.10.csv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD073177/kinesin_mScarlet_separated_Linear_PSM_xiFDR2.3.10.csv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD073177/kinesin_mScarlet_separated_CSM_xiFDR2.3.10.csv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD073177/kinesin_mScarlet_separated_Linear_Peptides_xiFDR2.3.10.csv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD073177/kinesin_mScarlet_separated_summary_xiFDR2.3.10.csv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD073177/kinesin_mScarlet_separated_Xi1.8.9.csv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD073177/kinesin_mScarlet_separated_Links_xiFDR2.3.10.csv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD073177/kinesin_total_XL_MS_peaks.csv.gz"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD073177/kinesin_total_XL_MS.raw"],"Mzid":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD073177/kinesin_mScarlet_separated.mzid.summary.csv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD073177/kinesin_mScarlet_separated.mzid","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD073177/kinesin_mScarlet_separated_cleaned.mzid"],"Mgf":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD073177/recal_kinesin_total_XL_MS.mgf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD073177/MS2_err_kinesin_total_XL_MS.mgf.png","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD073177/MS1_err_kinesin_total_XL_MS.mgf.png","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD073177/kinesin_total_XL_MS.mgf"],"Fasta":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD073177/kinesin_mScarlet_separate.fasta"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD073177/kinesin_mScarlet_separated_Xi1.8.9.config"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["sdfried@jhu.edu"],"submitter":["Yuqi Tang"],"technology_type":["Mass Spectrometry","Chemical cross-linking coupled with mass spectrometry proteomics"],"software":["Not available"],"submitter_keywords":["Kinesin-1","Plus-end directed","Microtubule motor","Motor protein","Cryo-em","Kif5b","Structure","Kinesin"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD073177"],"sample_protocol":["Kinesin KIF5B-mScarlet-KLC1 heterotetramer was crosslinked with 0.5-2 mM BS3 at 4C overnight using sucrose density gradient.  The crosslinked samples were the denatured (8 M urea), reduced (5 mM DTT), alkylated (15 mM IAA), quenched with DTT, digested with LysC (1:100 w:w ratio), diluted 4-fold, digested with trypsin (1:50 w:w ratio), desalted (Sep-Pak C18), and vacuum-dried. The sample was analyzed using an UltiMate3000 UHPLC system coupled to a Q-Exactive HF-X Orbitrap. Peptides were resuspended and loaded onto PepMap 100 C18 column with Solvent A (0.1% formic acid in water) and solvent B (0.1% formic acid in 98% ACN). Then the peptides were separated using PepMap RSLC C18 column with a linear gradient from 5% to 25% solvent B over 100 min, then to 45% over 25 min, and to 90% over 5 min. For LC-MS/MS data acquisition, the Q-Exactive HF-X performed MS1 scans at 120,000 resolution (350-1500 m/z), AGC target of 3 × 106, and 50 ms max IT. The top 10 precursors (z = 3-8) were isolated (1.4 m/z window) and fragmented using stepped NCE (323). MS2 scans were at 60,000 resolution (200-2000 m/z), AGC target of 1 × 105, and 150 ms max IT. Dynamic exclusion was set to 45 s and in-source CID at 10 eV."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["RAW file was converted and recalibrated using the xiSEARCH preprocessing pipeline python script. The recalibrated MGF file was searched with xiSEARCH 1.8.9 for crosslinked peptides. Search parameters were used as following: MS1 mass tolerance, 6 ppm; MS2 mass tolerance, 10 ppm; allowed maximum number of missed cleavages, 4; minimum peptide length, 6. Crosslinks were searched based on the modifications at Lys and N-term (preferred), modifications at Ser, Thr, and Tyr were also allowed with lower priority. Carbamidomethylations (+57.021464 Da) on Cys were enforced as fixed modifications, oxidations (+15.99491463 Da) on Met and phosphorylations on Ser/Thr/Tyr (Sp: + 166.9984 Da; Tp: +181.0140 Da; Yp: +243.0269 Da) were allowed as variable modifications. FASTA file containing KIF5B,KLC1 and mScarlet was applied in the search separately. Search results were filtered in xiFDR 2.3.10 at the residue pair level to an FDR of 5%. The boost function was enabled between residue pairs, and the rest of the settings were default. The mzid file generated from xiFDR was uploaded onto xiVIEW and PDB file generated from cryo-EM study was imported for crosslink visualization."],"omics_type":["Proteomics"],"labhead":["Stephen D. Fried"],"instrument_platform":[""],"submission_type":["COMPLETE"],"labhead_affiliation":["Associate Professor, Department of Chemistry Associate Professor, Thomas C. Jenkins Department of Biophysics Associate Professor, Department of Biology"],"species":["Escherichia Coli"],"submitter_mail":["ytang93@jh.edu"],"publication":["Not available"],"submitter_affiliation":["Johns Hopkins University"],"submitter_country":["United States"],"doi":["10.6019/PXD073177"],"additional_accession":[]},"is_claimable":false,"name":"Structural Basis of Kinesin-1 Autoinhibition and Its Control of Microtubule-Based Motility","description":"Kinesin-1 is the first identified microtubule-based motor protein that drives anterograde intracellular transport of diverse cargoes in eukaryotic cells. Defects in kinesin-1 activity have been implicated in various human neurological disorders and intracellular pathogens such as bacteria and viruses hijack its activity. Despite its importance, the molecular mechanisms governing kinesin-1 activation remains poorly understood. Here, we report a 8.6-Å cryo-EM electron microscopy structure of the autoinhibited kinesin-1 heterotetramer. Our structure reveals a complex 36-nm head-to-tail assembly composed of two kinesin heavy chains (KHC) and two light chains (KLC), where the self-folded dimeric KHCs are stabilized by asymmetrically arranged KLCs tetratricopeptide repeat (TPR) domains. This state inhibits kinesin motility by constraining the dimeric motor domains in a configuration that is incompatible with motility. Notably, our structure also shows that the dimeric KLC TPR cargo-binding domains are occluded, providing a structural basis for the autoinhibition of both motor activity and cargo binding.In addition to functional studies, we also applied crosslinking mass spectrometry (XLMS) to validate the autoinhibitory 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