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- PDB-4uxt: Conserved mechanisms of microtubule-stimulated ADP release, ATP b... -

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Basic information

Entry
Database: PDB / ID: 4uxt
TitleConserved mechanisms of microtubule-stimulated ADP release, ATP binding, and force generation in transport kinesins
Components
  • KINESIN HEAVY CHAIN ISOFORM 5A
  • TUBULIN ALPHA-1B CHAIN
  • TUBULIN BETA-2B CHAIN
KeywordsTRANSPORT PROTEIN
Function / homology
Function and homology information


anterograde dendritic transport of neurotransmitter receptor complex / retrograde neuronal dense core vesicle transport / anterograde axonal protein transport / plus-end-directed microtubule motor activity / RHO GTPases activate KTN1 / Kinesins / positive regulation of axon guidance / kinesin complex / COPI-dependent Golgi-to-ER retrograde traffic / ciliary rootlet ...anterograde dendritic transport of neurotransmitter receptor complex / retrograde neuronal dense core vesicle transport / anterograde axonal protein transport / plus-end-directed microtubule motor activity / RHO GTPases activate KTN1 / Kinesins / positive regulation of axon guidance / kinesin complex / COPI-dependent Golgi-to-ER retrograde traffic / ciliary rootlet / microtubule-based movement / synaptic vesicle transport / Insulin processing / cytoskeletal motor activity / kinesin binding / postsynaptic cytosol / cytoplasmic microtubule / microtubule-based process / axon cytoplasm / vesicle-mediated transport / MHC class II antigen presentation / dendrite cytoplasm / cellular response to interleukin-4 / axon guidance / structural constituent of cytoskeleton / microtubule cytoskeleton organization / microtubule cytoskeleton / mitotic cell cycle / double-stranded RNA binding / nervous system development / microtubule binding / Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement / chemical synaptic transmission / perikaryon / microtubule / protein heterodimerization activity / GTPase activity / ubiquitin protein ligase binding / GTP binding / perinuclear region of cytoplasm / ATP hydrolysis activity / ATP binding / membrane / metal ion binding / cytosol / cytoplasm
Similarity search - Function
Kinesin-like protein / Kinesin motor domain signature. / Kinesin motor domain, conserved site / Kinesin motor domain / Kinesin motor domain profile. / Kinesin motor, catalytic domain. ATPase. / Kinesin motor domain / Kinesin motor domain superfamily / Alpha tubulin / Tubulin-beta mRNA autoregulation signal. ...Kinesin-like protein / Kinesin motor domain signature. / Kinesin motor domain, conserved site / Kinesin motor domain / Kinesin motor domain profile. / Kinesin motor, catalytic domain. ATPase. / Kinesin motor domain / Kinesin motor domain superfamily / Alpha tubulin / Tubulin-beta mRNA autoregulation signal. / Beta tubulin, autoregulation binding site / Beta tubulin / Tubulin / Tubulin, C-terminal / Tubulin C-terminal domain / Tubulin, conserved site / Tubulin subunits alpha, beta, and gamma signature. / Tubulin/FtsZ family, C-terminal domain / Tubulin/FtsZ-like, C-terminal domain / Tubulin/FtsZ, C-terminal / Tubulin/FtsZ, 2-layer sandwich domain / Tubulin/FtsZ family, GTPase domain / Tubulin/FtsZ family, GTPase domain / Tubulin/FtsZ, GTPase domain / Tubulin/FtsZ, GTPase domain superfamily / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
GUANOSINE-5'-DIPHOSPHATE / GUANOSINE-5'-TRIPHOSPHATE / TAXOL / Tubulin alpha-1B chain / Kinesin heavy chain isoform 5A / Tubulin beta-2B chain
Similarity search - Component
Biological speciesHOMO SAPIENS (human)
BOS TAURUS (domestic cattle)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 7.4 Å
Model type detailsCA ATOMS ONLY, CHAIN A, B, C
AuthorsAtherton, J. / Farabella, I. / Yu, I.M. / Rosenfeld, S.S. / Houdusse, A. / Topf, M. / Moores, C.
CitationJournal: Elife / Year: 2014
Title: Conserved mechanisms of microtubule-stimulated ADP release, ATP binding, and force generation in transport kinesins.
Authors: Joseph Atherton / Irene Farabella / I-Mei Yu / Steven S Rosenfeld / Anne Houdusse / Maya Topf / Carolyn A Moores /
Abstract: Kinesins are a superfamily of microtubule-based ATP-powered motors, important for multiple, essential cellular functions. How microtubule binding stimulates their ATPase and controls force generation ...Kinesins are a superfamily of microtubule-based ATP-powered motors, important for multiple, essential cellular functions. How microtubule binding stimulates their ATPase and controls force generation is not understood. To address this fundamental question, we visualized microtubule-bound kinesin-1 and kinesin-3 motor domains at multiple steps in their ATPase cycles--including their nucleotide-free states--at ∼ 7 Å resolution using cryo-electron microscopy. In both motors, microtubule binding promotes ordered conformations of conserved loops that stimulate ADP release, enhance microtubule affinity and prime the catalytic site for ATP binding. ATP binding causes only small shifts of these nucleotide-coordinating loops but induces large conformational changes elsewhere that allow force generation and neck linker docking towards the microtubule plus end. Family-specific differences across the kinesin-microtubule interface account for the distinctive properties of each motor. Our data thus provide evidence for a conserved ATP-driven mechanism for kinesins and reveal the critical mechanistic contribution of the microtubule interface.
History
DepositionAug 27, 2014Deposition site: PDBE / Processing site: PDBE
Revision 1.0Sep 24, 2014Provider: repository / Type: Initial release
Revision 1.1Oct 22, 2014Group: Database references
Revision 1.2Aug 23, 2017Group: Data collection / Refinement description / Category: em_3d_fitting / em_software
Item: _em_3d_fitting.target_criteria / _em_software.fitting_id ..._em_3d_fitting.target_criteria / _em_software.fitting_id / _em_software.image_processing_id / _em_software.name
Revision 1.3May 8, 2024Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / em_3d_fitting_list / pdbx_initial_refinement_model / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _em_3d_fitting_list.accession_code / _em_3d_fitting_list.initial_refinement_model_id / _em_3d_fitting_list.source_name / _em_3d_fitting_list.type / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

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Structure visualization

Movie
  • Deposited structure unit
  • Imaged by Jmol
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  • Simplified surface model + fitted atomic model
  • EMDB-2769
  • Imaged by Jmol
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  • Superimposition on EM map
  • EMDB-2769
  • Imaged by UCSF Chimera
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Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: TUBULIN ALPHA-1B CHAIN
B: TUBULIN BETA-2B CHAIN
C: KINESIN HEAVY CHAIN ISOFORM 5A
hetero molecules


Theoretical massNumber of molelcules
Total (without water)139,9558
Polymers138,0453
Non-polymers1,9105
Water00
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA

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Components

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Protein , 3 types, 3 molecules ABC

#1: Protein TUBULIN ALPHA-1B CHAIN / ALPHA-TUBULIN UBIQUITOUS / TUBULIN K-ALPHA-1 / TUBULIN ALPHA- UBIQUITOUS CHAIN / Coordinate model: Cα atoms only


Mass: 50107.238 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) BOS TAURUS (domestic cattle) / References: UniProt: P81947
#2: Protein TUBULIN BETA-2B CHAIN / Coordinate model: Cα atoms only


Mass: 49907.770 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) BOS TAURUS (domestic cattle) / References: UniProt: Q6B856
#3: Protein KINESIN HEAVY CHAIN ISOFORM 5A / KINESIN HEAVY CHAIN NEURON-SPECIFIC 1 / NEURONAL KINESIN HEAVY CHAIN / NKHC / Coordinate model: Cα atoms only


Mass: 38030.184 Da / Num. of mol.: 1 / Fragment: MOTOR DOMAIN, UNP RESIDUES 1-340
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) HOMO SAPIENS (human) / Plasmid: PET151-D-TOPO / Production host: ESCHERICHIA COLI (E. coli) / References: UniProt: Q12840

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Non-polymers , 5 types, 5 molecules

#4: Chemical ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Zn
#5: Chemical ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Mg
#6: Chemical ChemComp-GTP / GUANOSINE-5'-TRIPHOSPHATE


Mass: 523.180 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C10H16N5O14P3 / Comment: GTP, energy-carrying molecule*YM
#7: Chemical ChemComp-GDP / GUANOSINE-5'-DIPHOSPHATE


Type: RNA linking / Mass: 443.201 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C10H15N5O11P2 / Comment: GDP, energy-carrying molecule*YM
#8: Chemical ChemComp-TA1 / TAXOL


Mass: 853.906 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C47H51NO14 / Comment: medication, chemotherapy*YM

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Experimental details

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Experiment

ExperimentMethod: ELECTRON MICROSCOPY
EM experimentAggregation state: FILAMENT / 3D reconstruction method: single particle reconstruction

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Sample preparation

ComponentName: 13-PROTOFILAMENT MICROTUBULE-BOUND HUMAN KINESIN-1 MOTOR DOMAIN IN ABSENCE OF NUCLEOTIDES
Type: COMPLEX
Buffer solutionName: 20MM PIPES, 2MM MGCL2, 1MM EGTA, 2MM DTT, 10 U/ML APYRASE
pH: 6.8
Details: 20MM PIPES, 2MM MGCL2, 1MM EGTA, 2MM DTT, 10 U/ML APYRASE
SpecimenEmbedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
Specimen supportDetails: HOLEY CARBON
VitrificationInstrument: FEI VITROBOT MARK I / Cryogen name: ETHANE / Details: LIQUID ETHANE

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Electron microscopy imaging

Experimental equipment
Model: Tecnai Polara / Image courtesy: FEI Company
MicroscopyModel: FEI POLARA 300 / Date: Dec 10, 2012
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELD / Calibrated magnification: 100000 X / Nominal defocus max: 3500 nm / Nominal defocus min: 400 nm / Cs: 2.3 mm
Specimen holderTemperature: 90 K
Image recordingElectron dose: 20 e/Å2 / Film or detector model: GATAN ULTRASCAN 4000 (4k x 4k)
Image scansNum. digital images: 497

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Processing

EM software
IDNameCategory
1Flex-EMmodel fitting
2UCSF Chimeramodel fitting
3FREALIGN3D reconstruction
4SPIDER3D reconstruction
CTF correctionDetails: FREALIGN
3D reconstructionResolution: 7.4 Å / Num. of particles: 168974 / Actual pixel size: 1.5 Å
Details: SUBMISSION BASED ON EXPERIMENTAL DATA FROM EMDB EMD-2769. (DEPOSITION ID: 12602).
Symmetry type: HELICAL
Atomic model buildingProtocol: FLEXIBLE FIT / Space: REAL / Target criteria: Cross-correlation coefficient / Details: METHOD--FLEXIBLE REFINEMENT PROTOCOL--X-RAY
Atomic model buildingPDB-ID: 1BG2

1bg2


Accession code: 1BG2 / Source name: PDB / Type: experimental model
RefinementHighest resolution: 7.4 Å
Refinement stepCycle: LAST / Highest resolution: 7.4 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1158 0 124 0 1282

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