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- PDB-1vfx: Crystal Structure of the Kif1A Motor Domain Complexed With ADP-Mg-AlFx -

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Basic information

Entry
Database: PDB / ID: 1vfx
TitleCrystal Structure of the Kif1A Motor Domain Complexed With ADP-Mg-AlFx
ComponentsPROTEIN (Fusion protein consisting of Kinesin-like protein KIF1A, Kinesin heavy chain isoform 5C and A HIS TAG
KeywordsTRANSPORT PROTEIN / kinesin / microtubule / motor
Function / homology
Function and homology information


anterograde dendritic transport of messenger ribonucleoprotein complex / distal axon / dendritic transport of messenger ribonucleoprotein complex / extrinsic component of neuronal dense core vesicle membrane / protein transport along microtubule / dense core granule cytoskeletal transport / interkinetic nuclear migration / neuronal dense core vesicle / anterograde neuronal dense core vesicle transport / Kinesins ...anterograde dendritic transport of messenger ribonucleoprotein complex / distal axon / dendritic transport of messenger ribonucleoprotein complex / extrinsic component of neuronal dense core vesicle membrane / protein transport along microtubule / dense core granule cytoskeletal transport / interkinetic nuclear migration / neuronal dense core vesicle / anterograde neuronal dense core vesicle transport / Kinesins / anterograde dendritic transport of neurotransmitter receptor complex / retrograde neuronal dense core vesicle transport / anterograde axonal protein transport / regulation of dendritic spine development / COPI-dependent Golgi-to-ER retrograde traffic / apolipoprotein receptor binding / cytoskeleton-dependent intracellular transport / regulation of dendritic spine morphogenesis / MHC class II antigen presentation / anterograde axonal transport / motor neuron axon guidance / synaptic vesicle transport / plus-end-directed microtubule motor activity / ciliary rootlet / microtubule motor activity / kinesin complex / ATP metabolic process / microtubule-based movement / axon cytoplasm / mRNA transport / axonal growth cone / presynapse / vesicle-mediated transport / dendrite cytoplasm / axon guidance / postsynapse / synaptic vesicle / microtubule binding / microtubule / neuron projection / axon / neuronal cell body / dendrite / perinuclear region of cytoplasm / protein-containing complex / ATP binding / identical protein binding / cytosol / cytoplasm
Similarity search - Function
Kinesin protein 1B / Kinesin-like KIF1-type / Kinesin protein / Kinesin-like / Kinesin-associated / Kinesin-associated / Kinesin-like protein / Kinesin motor domain / Kinesin / Forkhead-associated (FHA) domain profile. ...Kinesin protein 1B / Kinesin-like KIF1-type / Kinesin protein / Kinesin-like / Kinesin-associated / Kinesin-associated / Kinesin-like protein / Kinesin motor domain / Kinesin / Forkhead-associated (FHA) domain profile. / Forkhead associated domain / FHA domain / Forkhead-associated (FHA) domain / Kinesin motor domain signature. / Kinesin motor domain, conserved site / Kinesin motor domain profile. / Kinesin motor, catalytic domain. ATPase. / Kinesin motor domain / Kinesin motor domain / SMAD/FHA domain superfamily / Kinesin motor domain superfamily / PH domain / PH domain profile. / Pleckstrin homology domain. / Pleckstrin homology domain / PH-like domain superfamily / P-loop containing nucleoside triphosphate hydrolase / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
Kinesin heavy chain isoform 5C / ADENOSINE-5'-DIPHOSPHATE / ALUMINUM FLUORIDE / Kinesin-like protein KIF1A
Similarity search - Component
Biological speciesMus musculus (house mouse)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.55 Å
AuthorsNitta, R. / Kikkawa, M. / Okada, Y. / Hirokawa, N.
CitationJournal: Science / Year: 2004
Title: KIF1A Alternately Uses Two Loops to Bind Microtubules
Authors: Nitta, R. / Kikkawa, M. / Okada, Y. / Hirokawa, N.
History
DepositionApr 19, 2004Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Aug 10, 2004Provider: repository / Type: Initial release
Revision 1.1Apr 27, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Aug 23, 2017Group: Source and taxonomy / Category: entity_src_gen

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: PROTEIN (Fusion protein consisting of Kinesin-like protein KIF1A, Kinesin heavy chain isoform 5C and A HIS TAG
hetero molecules


Theoretical massNumber of molelcules
Total (without water)41,9086
Polymers41,1281
Non-polymers7805
Water1,49583
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
γ
α
β
Length a, b, c (Å)41.934, 54.649, 156.784
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121

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Components

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Protein , 1 types, 1 molecules A

#1: Protein PROTEIN (Fusion protein consisting of Kinesin-like protein KIF1A, Kinesin heavy chain isoform 5C and A HIS TAG / Axonal transporter of synaptic vesicles


Mass: 41128.215 Da / Num. of mol.: 1
Fragment: Motor Domain OF Kinesin-like protein KIF1A and RESIDUES 329-334 OF Kinesin heavy chain isoform 5C
Source method: isolated from a genetically manipulated source
Details: FUSION PROTEIN COMPRISES RESIDUES 1-355 OF Kinesin-like protein KIF1A, AND RESIDUES 329-334 OF Kinesin heavy chain isoform 5C, AND C-TERMINAL TAIL WITH SEQUENCE HHHHH
Source: (gene. exp.) Mus musculus (house mouse) / Plasmid: pET-21b / Production host: Escherichia coli (E. coli) / References: UniProt: P33173, UniProt: P28738

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Non-polymers , 5 types, 88 molecules

#2: Chemical ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Mg
#3: Chemical ChemComp-AF3 / ALUMINUM FLUORIDE / Aluminium fluoride


Mass: 83.977 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: AlF3
#4: Chemical ChemComp-TRS / 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL / TRIS BUFFER / Tris


Mass: 122.143 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C4H12NO3 / Comment: pH buffer*YM
#5: Chemical ChemComp-ADP / ADENOSINE-5'-DIPHOSPHATE / Adenosine diphosphate


Mass: 427.201 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C10H15N5O10P2 / Comment: ADP, energy-carrying molecule*YM
#6: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 83 / Source method: isolated from a natural source / Formula: H2O

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

CrystalDensity Matthews: 2.32 Å3/Da / Density % sol: 46.99 %
Crystal growTemperature: 297 K / Method: vapor diffusion, hanging drop / pH: 8.5
Details: PEG4000, Sodium acetate, Tris-HCl, Xylitol, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 297.0K

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Data collection

DiffractionMean temperature: 93 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 19-ID / Wavelength: 1.03 Å
DetectorType: SBC-2 / Detector: CCD / Date: Jul 28, 2002
RadiationMonochromator: DOUBLE CRYSTAL SI220 / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.03 Å / Relative weight: 1
ReflectionResolution: 2.55→50 Å / Num. all: 12385 / Num. obs: 9351 / % possible obs: 75.5 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Biso Wilson estimate: 36.4 Å2
Reflection shellResolution: 2.55→2.64 Å / % possible all: 69.5

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Processing

Software
NameVersionClassification
CNS1refinement
HKL-2000data reduction
SCALEPACKdata scaling
CNSphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.55→22.18 Å / Rfactor Rfree error: 0.01 / Data cutoff high absF: 1166240.52 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber
RfactorNum. reflection% reflectionSelection details
Rfree0.294 932 10.2 %RANDOM
Rwork0.238 ---
all0.266 12341 --
obs0.238 9145 74.1 %-
Solvent computationSolvent model: FLAT MODEL / Bsol: 62.7999 Å2 / ksol: 0.337431 e/Å3
Displacement parametersBiso mean: 59.2 Å2
Baniso -1Baniso -2Baniso -3
1--9.76 Å20 Å20 Å2
2--39.54 Å20 Å2
3----29.78 Å2
Refine analyze
FreeObs
Luzzati coordinate error0.5 Å0.38 Å
Luzzati d res low-24 Å
Luzzati sigma a0.61 Å0.41 Å
Refinement stepCycle: LAST / Resolution: 2.55→22.18 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms2553 0 48 83 2684
Refine LS restraints
Refine-IDTypeDev idealDev ideal target
X-RAY DIFFRACTIONc_bond_d0.01
X-RAY DIFFRACTIONc_angle_deg1.9
X-RAY DIFFRACTIONc_dihedral_angle_d25.7
X-RAY DIFFRACTIONc_improper_angle_d1.42
X-RAY DIFFRACTIONc_mcbond_it3.61.5
X-RAY DIFFRACTIONc_mcangle_it5.612
X-RAY DIFFRACTIONc_scbond_it5.422
X-RAY DIFFRACTIONc_scangle_it7.752.5
LS refinement shellResolution: 2.55→2.71 Å / Rfactor Rfree error: 0.036 / Total num. of bins used: 6
RfactorNum. reflection% reflection
Rfree0.413 128 9.7 %
Rwork0.352 1193 -
obs--65.8 %
Xplor file
Refine-IDSerial noParam fileTopol file
X-RAY DIFFRACTION1PROTEIN_REP.PARAMPROTEIN.TOP
X-RAY DIFFRACTION2LIGAND.PARAMLIGAND.TOP
X-RAY DIFFRACTION3ION.PARAMION.TOP
X-RAY DIFFRACTION4WATER_REP.PARAMWATER_REP.TOP
X-RAY DIFFRACTION5TRS.PARAMTRS.TOP

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