{"EMPIAR-10382":{"imagesets":[{"segmentations":[],"name":"Unaligned multi-frame movies of ADPBeFx-bound Spastin","directory":"data","category":"micrographs - multiframe","header_format":"MRC","data_format":"MRC","num_images_or_tilt_series":1200,"frames_per_image":49,"frame_range_min":2,"frame_range_max":49,"voxel_type":"SIGNED 16 BIT INTEGER","pixel_width":1.056,"pixel_height":1.056,"micrographs_file_pattern":"data/FoilHole_16483990_Data_16480075_16480076_20181118_1720_Fractions.mrc","picked_particles_file_pattern":"data/FoilHole_16483990_Data_16480075_16480076_20181118_1720_Fractions.mrc","picked_particles_directory":"data","details":"Unaligned multi-frame movies of ADPBeFx-bound Spastin","image_width":"4096","image_height":"4096"}],"workflow_file":null,"grant_references":[],"version_history":[],"title":"Structure of spastin bound to a glutamate-rich peptide implies a hand-over-hand mechanism of substrate translocation.","principal_investigator":[{"author_orcid":"0000-0001-6796-7740","middle_name":"P","organization":"University of Utah, Department of Biochemistry","street":"15 N Medical Drive East","town_or_city":"Salt Lake City","state_or_province":"Utah","post_or_zip":"84112","telephone":"+1 801 585 9776","fax":"+1 801 581 7959","first_name":"Christopher","last_name":"Hill","email":"chris [at] biochem.utah.edu","country":"United States","entry":"EMPIAR-10382"}],"status":"REL","deposition_date":"2020-03-04","release_date":"2021-01-29","obsolete_date":null,"update_date":"2021-02-04","corresponding_author":{"author":{"author_orcid":"0000-0003-1762-8390","middle_name":"Linda","organization":"University of Utah, Department of Biochemistry","street":"15 N Medical Drive East","town_or_city":"Salt Lake City","state_or_province":"Utah","post_or_zip":"84112","first_name":"Heidi","last_name":"Schubert","country":"United States"}},"authors":[{"author":{"name":"Han H","author_orcid":"0000-0003-0361-4254"}},{"author":{"name":"Schubert HL","author_orcid":"0000-0003-1762-8390"}},{"author":{"name":"Purdy MD","author_orcid":"0000-0003-0189-933X"}},{"author":{"name":"Yeager M","author_orcid":"0000-0002-3301-640X"}},{"author":{"name":"Sundquist WI","author_orcid":"0000-0001-9988-6021"}},{"author":{"name":"Hill CP","author_orcid":"0000-0001-6796-7740"}}],"cross_references":["EMD-20327"],"biostudies_references":[],"idr_references":[],"empiar_references":[],"citation":[{"authors":[{"name":"Han H","author_orcid":"0000-0003-0361-4254"},{"name":"Schubert HL","author_orcid":"0000-0003-1762-8390"},{"name":"McCullough J","author_orcid":"0000-0001-6836-4394"},{"name":"Monroe N","author_orcid":"0000-0001-7678-4997"},{"name":"Purdy MD","author_orcid":"0000-0003-0189-933X"},{"name":"Yeager M","author_orcid":"0000-0002-3301-640X"},{"name":"Sundquist WI","author_orcid":"0000-0001-9988-6021"},{"name":"Hill CP","author_orcid":"0000-0001-6796-7740"}],"editors":[],"published":true,"j_or_nj_citation":true,"title":"Structure of spastin bound to a glutamate-rich peptide implies a hand-over-hand mechanism of substrate translocation.","volume":"2","country":"United States","first_page":"435","last_page":"443","year":"2019","language":"English","doi":"10.1074/jbc.AC119.009890","pubmedid":"31767681","details":"Many members of the AAA+ ATPase family function as hexamers that unfold their protein substrates. These AAA unfoldases include spastin, which plays a critical role in the architecture of eukaryotic cells by driving the remodeling and severing of microtubules, which are cytoskeletal polymers of tubulin subunits. Here, we demonstrate that a human spastin binds weakly to unmodified peptides from the C-terminal segment of human tubulin α1A/B. A peptide comprising alternating glutamate and tyrosine residues binds more tightly, which is consistent with the known importance of glutamylation for spastin microtubule severing activity. A cryo-EM structure of the spastin-peptide complex at 4.2 Å resolution revealed an asymmetric hexamer in which five spastin subunits adopt a helical, spiral staircase configuration that binds the peptide within the central pore, whereas the sixth subunit of the hexamer is displaced from the peptide/substrate, as if transitioning from one end of the helix to the other. This configuration differs from a recently published structure of spastin from Drosophila melanogaster, which forms a six-subunit spiral without a transitioning subunit. Our structure resembles other recently reported AAA unfoldases, including the meiotic clade relative Vps4, and supports a model in which spastin utilizes a hand-over-hand mechanism of tubulin translocation and microtubule remodeling.","book_chapter_title":null,"publisher":null,"publication_location":null,"journal":"Journal of Biological Chemistry","journal_abbreviation":"J Biol Chem","issue":"295","preprint":false}],"dataset_size":"1.8 TB","experiment_type":"EMDB","scale":null,"related_pdb_entries":["6pek"],"entry_doi":"10.6019/EMPIAR-10382"}}