Katanin spiral and ring structures shed light on power stroke for microtubule severing

Using a combination of crystallography, SAXS and cryo-EM, the katanin hexamer is observed in spiral or ring arrangements, suggesting a mechanism to generate the power stroke to severe microtubules. Microtubule-severing enzymes katanin, spastin and fidgetin are AAA ATPases important for the biogenesi...

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Published inNature structural & molecular biology Vol. 24; no. 9; pp. 717 - 725
Main Authors Zehr, Elena, Szyk, Agnieszka, Piszczek, Grzegorz, Szczesna, Ewa, Zuo, Xiaobing, Roll-Mecak, Antonina
Format Journal Article
LanguageEnglish
Published New York Nature Publishing Group US 01.09.2017
Nature Publishing Group
Subjects
60 APPLIED LIFE SCIENCES
631/535/1258/1259
631/535/1261
631/535/1266
631/80/128/2343
82
Adenosine Triphosphatases - chemistry
Adenosine Triphosphatases - metabolism
Adenosine Triphosphatases - ultrastructure
Adenosine Triphosphate - metabolism
Animals
ATPases
Axons
BASIC BIOLOGICAL SCIENCES
Biochemistry
Biological Microscopy
Caenorhabditis elegans - enzymology
Cilia
Cryoelectron Microscopy
Crystal structure
Crystallography, X-Ray
Enzymes
Gating
Interfaces
Katanin
Life Sciences
Membrane Biology
Microtubules
Models, Molecular
Protein Binding
Protein Conformation
protein SAXS
Protein Structure
Ring structures
Spindles
Stroke
Structural members
Online AccessGet full text

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Abstract Using a combination of crystallography, SAXS and cryo-EM, the katanin hexamer is observed in spiral or ring arrangements, suggesting a mechanism to generate the power stroke to severe microtubules. Microtubule-severing enzymes katanin, spastin and fidgetin are AAA ATPases important for the biogenesis and maintenance of complex microtubule arrays in axons, spindles and cilia. Because of a lack of known 3D structures for these enzymes, their mechanism of action has remained poorly understood. Here we report the X-ray crystal structure of the monomeric AAA katanin module from Caenorhabditis elegans and cryo-EM reconstructions of the hexamer in two conformations. The structures reveal an unexpected asymmetric arrangement of the AAA domains mediated by structural elements unique to microtubule-severing enzymes and critical for their function. The reconstructions show that katanin cycles between open spiral and closed ring conformations, depending on the ATP occupancy of a gating protomer that tenses or relaxes interprotomer interfaces. Cycling of the hexamer between these conformations would provide the power stroke for microtubule severing.
AbstractList Microtubule-severing enzymes katanin, spastin and fidgetin are AAA ATPases important for the biogenesis and maintenance of complex microtubule arrays in axons, spindles and cilia. Because of a lack of 3D structures, their mechanism has remained poorly understood. Here we report the first X-ray structure of the monomeric AAA katanin module and cryo-EM reconstructions of the hexamer in two conformations. These reveal an unexpected asymmetric arrangement of the AAA domains mediated by structural elements unique to severing enzymes and critical for their function. Our reconstructions show that katanin cycles between open spiral and closed ring conformations, depending on the ATP occupancy of a gating protomer that tenses or relaxes inter-protomer interfaces. Cycling of the hexamer between these conformations would provide the power stroke for microtubule severing.
Microtubule-severing enzymes katanin, spastin and fidgetin are AAA ATPases important for the biogenesis and maintenance of complex microtubule arrays in axons, spindles and cilia. Because of a lack of known 3D structures for these enzymes, their mechanism of action has remained poorly understood. Here we report the X-ray crystal structure of the monomeric AAA katanin module from Caenorhabditis elegans and cryo-EM reconstructions of the hexamer in two conformations. The structures reveal an unexpected asymmetric arrangement of the AAA domains mediated by structural elements unique to microtubule-severing enzymes and critical for their function. The reconstructions show that katanin cycles between open spiral and closed ring conformations, depending on the ATP occupancy of a gating protomer that tenses or relaxes interprotomer interfaces. Cycling of the hexamer between these conformations would provide the power stroke for microtubule severing.
Using a combination of crystallography, SAXS and cryo-EM, the katanin hexamer is observed in spiral or ring arrangements, suggesting a mechanism to generate the power stroke to severe microtubules. Microtubule-severing enzymes katanin, spastin and fidgetin are AAA ATPases important for the biogenesis and maintenance of complex microtubule arrays in axons, spindles and cilia. Because of a lack of known 3D structures for these enzymes, their mechanism of action has remained poorly understood. Here we report the X-ray crystal structure of the monomeric AAA katanin module from Caenorhabditis elegans and cryo-EM reconstructions of the hexamer in two conformations. The structures reveal an unexpected asymmetric arrangement of the AAA domains mediated by structural elements unique to microtubule-severing enzymes and critical for their function. The reconstructions show that katanin cycles between open spiral and closed ring conformations, depending on the ATP occupancy of a gating protomer that tenses or relaxes interprotomer interfaces. Cycling of the hexamer between these conformations would provide the power stroke for microtubule severing.
Microtubule-severing enzymes katanin, spastin and fidgetin are AAA ATPases important for the biogenesis and maintenance of complex microtubule arrays in axons, spindles and cilia. Because of a lack of known 3D structures for these enzymes, their mechanism of action has remained poorly understood. Here we report the X-ray crystal structure of the monomeric AAA katanin module from Caenorhabditis elegans and cryo-EM reconstructions of the hexamer in two conformations. The structures reveal an unexpected asymmetric arrangement of the AAA domains mediated by structural elements unique to microtubule-severing enzymes and critical for their function. The reconstructions show that katanin cycles between open spiral and closed ring conformations, depending on the ATP occupancy of a gating protomer that tenses or relaxes interprotomer interfaces. Cycling of the hexamer between these conformations would provide the power stroke for microtubule severing.Microtubule-severing enzymes katanin, spastin and fidgetin are AAA ATPases important for the biogenesis and maintenance of complex microtubule arrays in axons, spindles and cilia. Because of a lack of known 3D structures for these enzymes, their mechanism of action has remained poorly understood. Here we report the X-ray crystal structure of the monomeric AAA katanin module from Caenorhabditis elegans and cryo-EM reconstructions of the hexamer in two conformations. The structures reveal an unexpected asymmetric arrangement of the AAA domains mediated by structural elements unique to microtubule-severing enzymes and critical for their function. The reconstructions show that katanin cycles between open spiral and closed ring conformations, depending on the ATP occupancy of a gating protomer that tenses or relaxes interprotomer interfaces. Cycling of the hexamer between these conformations would provide the power stroke for microtubule severing.
Microtubule-severing enzymes katanin, spastin and fidgetin are AAA ATPases critical for the biogenesis and maintenance of complex microtubule arrays in axons, spindles and cilia. Because of a lack of 3D structures, their mechanism has remained poorly understood. We report the first X-ray structure of the monomeric AAA katanin module and cryo-EM reconstructions of the hexamer in two conformations. These reveal an unexpected asymmetric arrangement of the AAA domains mediated by structural elements unique to severing enzymes and critical for their function. Our reconstructions show that katanin cycles between open spiral and closed ring conformations, depending on the ATP occupancy of a gating protomer that tenses or relaxes inter-protomer interfaces. Cycling of the hexamer between these conformations would provide the power stroke for microtubule severing.
Audience Academic
Author Zuo, Xiaobing
Piszczek, Grzegorz
Roll-Mecak, Antonina
Szyk, Agnieszka
Zehr, Elena
Szczesna, Ewa
AuthorAffiliation 3 X-Ray Science Division, Advanced Photon Source, Argonne National Laboratory, Argonne, Illinois
2 Biophysics Core, National Heart, Lung and Blood Institute, Bethesda, Maryland, U.S.A
1 Cell Biology and Biophysics Unit, Porter Neuroscience Research Center, National Institute of Neurological Disorders and Stroke, Bethesda, Maryland, U.S.A
AuthorAffiliation_xml – name: 3 X-Ray Science Division, Advanced Photon Source, Argonne National Laboratory, Argonne, Illinois
– name: 2 Biophysics Core, National Heart, Lung and Blood Institute, Bethesda, Maryland, U.S.A
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  surname: Zehr
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  organization: Cell Biology and Biophysics Unit, Porter Neuroscience Research Center, National Institute of Neurological Disorders and Stroke
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  givenname: Agnieszka
  surname: Szyk
  fullname: Szyk, Agnieszka
  organization: Cell Biology and Biophysics Unit, Porter Neuroscience Research Center, National Institute of Neurological Disorders and Stroke
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  givenname: Grzegorz
  surname: Piszczek
  fullname: Piszczek, Grzegorz
  organization: Biophysics Core, National Heart, Lung and Blood Institute
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  givenname: Ewa
  surname: Szczesna
  fullname: Szczesna, Ewa
  organization: Cell Biology and Biophysics Unit, Porter Neuroscience Research Center, National Institute of Neurological Disorders and Stroke
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  givenname: Xiaobing
  surname: Zuo
  fullname: Zuo, Xiaobing
  organization: X-ray Science Division, Advanced Photon Source, Argonne National Laboratory
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  givenname: Antonina
  orcidid: 0000-0003-2621-7307
  surname: Roll-Mecak
  fullname: Roll-Mecak, Antonina
  email: Antonina@mail.nih.gov
  organization: Cell Biology and Biophysics Unit, Porter Neuroscience Research Center, National Institute of Neurological Disorders and Stroke, Biochemistry and Biophysics Center, National Heart, Lung and Blood Institute
BackLink https://www.ncbi.nlm.nih.gov/pubmed/28783150$$D View this record in MEDLINE/PubMed
https://www.osti.gov/servlets/purl/1394618$$D View this record in Osti.gov
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ISSN 1545-9993
1545-9985
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Fri Jul 25 09:03:10 EDT 2025
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content type line 14
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AC02-06CH11357
USDOE Office of Science (SC), Basic Energy Sciences (BES)
AUTHOR CONTRIBUTIONS
E.Z. prepared grids, collected and processed EM data with input from A.R.-M. The high-resolution dataset was collected at Janelia Research Campus (Howard Hughes Medical Institute). All EM data were processed on the Biowulf cluster at the National Institutes of Health. A.R.-M. and E.Z. built and refined models. A.S. purified proteins, obtained crystals, collected X-ray diffraction and SAXS data and performed ATP binding and ATP hydrolysis assays. G.P. performed and interpreted AUC. E.W. performed in vitro severing assays. X.Z. collected and processed SAXS data. A.R.-M. refined X-ray structure. A.R.-M. and E.Z. wrote manuscript. All authors reviewed the manuscript. A.R.-M. conceived project and supervised research.
ORCID 0000-0003-2621-7307
0000000326217307
OpenAccessLink https://www.osti.gov/servlets/purl/1394618
PMID 28783150
PQID 1936256177
PQPubID 27587
PageCount 9
ParticipantIDs pubmedcentral_primary_oai_pubmedcentral_nih_gov_7152510
osti_scitechconnect_1394618
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PublicationTitleAbbrev Nat Struct Mol Biol
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Snippet Using a combination of crystallography, SAXS and cryo-EM, the katanin hexamer is observed in spiral or ring arrangements, suggesting a mechanism to generate...
Microtubule-severing enzymes katanin, spastin and fidgetin are AAA ATPases important for the biogenesis and maintenance of complex microtubule arrays in axons,...
Microtubule-severing enzymes katanin, spastin and fidgetin are AAA ATPases critical for the biogenesis and maintenance of complex microtubule arrays in axons,...
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StartPage 717
SubjectTerms 60 APPLIED LIFE SCIENCES
631/535/1258/1259
631/535/1261
631/535/1266
631/80/128/2343
82
Adenosine Triphosphatases - chemistry
Adenosine Triphosphatases - metabolism
Adenosine Triphosphatases - ultrastructure
Adenosine Triphosphate - metabolism
Animals
ATPases
Axons
BASIC BIOLOGICAL SCIENCES
Biochemistry
Biological Microscopy
Caenorhabditis elegans - enzymology
Cilia
Cryoelectron Microscopy
Crystal structure
Crystallography, X-Ray
Enzymes
Gating
Interfaces
Katanin
Life Sciences
Membrane Biology
Microtubules
Models, Molecular
Protein Binding
Protein Conformation
protein SAXS
Protein Structure
Ring structures
Spindles
Stroke
Structural members
Title Katanin spiral and ring structures shed light on power stroke for microtubule severing
URI https://link.springer.com/article/10.1038/nsmb.3448
https://www.ncbi.nlm.nih.gov/pubmed/28783150
https://www.proquest.com/docview/1936256177
https://www.proquest.com/docview/1926978978
https://www.osti.gov/servlets/purl/1394618
https://pubmed.ncbi.nlm.nih.gov/PMC7152510
Volume 24
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