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Basic information

Entry
Database: PDB / ID: 1v8k
TitleThe Crystal Structure of the Minimal Functional Domain of the Microtubule Destabilizer KIF2C Complexed with Mg-AMPPNP
ComponentsKinesin-like protein KIF2C
KeywordsSTRUCTURAL PROTEIN / Kinesin-Like Protein / Microtubule Destabilizer
Function / homology
Function and homology information


regulation of chromosome segregation / establishment or maintenance of microtubule cytoskeleton polarity / Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal / metaphase chromosome alignment / Kinesins / Mitotic Prometaphase / EML4 and NUDC in mitotic spindle formation / Resolution of Sister Chromatid Cohesion / COPI-dependent Golgi-to-ER retrograde traffic / RHO GTPases Activate Formins ...regulation of chromosome segregation / establishment or maintenance of microtubule cytoskeleton polarity / Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal / metaphase chromosome alignment / Kinesins / Mitotic Prometaphase / EML4 and NUDC in mitotic spindle formation / Resolution of Sister Chromatid Cohesion / COPI-dependent Golgi-to-ER retrograde traffic / RHO GTPases Activate Formins / Separation of Sister Chromatids / microtubule plus-end / attachment of mitotic spindle microtubules to kinetochore / MHC class II antigen presentation / microtubule plus-end binding / microtubule depolymerization / microtubule motor activity / kinesin complex / mitotic metaphase chromosome alignment / microtubule-based movement / chromosome, centromeric region / kinetochore / spindle / microtubule binding / microtubule / cell division / centrosome / ATP hydrolysis activity / ATP binding / nucleus / cytoplasm
Similarity search - Function
Kinesin motor domain / Kinesin / 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 ...Kinesin motor domain / Kinesin / 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 / P-loop containing nucleoside triphosphate hydrolase / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER / Kinesin-like protein KIF2C
Similarity search - Component
Biological speciesMus musculus (house mouse)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.25 Å
AuthorsOgawa, T. / Nitta, R. / Okada, Y. / Hirokawa, N.
CitationJournal: Cell(Cambridge,Mass.) / Year: 2004
Title: A common mechanism for microtubule destabilizers-M type kinesins stabilize curling of the protofilament using the class-specific neck and loops.
Authors: Ogawa, T. / Nitta, R. / Okada, Y. / Hirokawa, N.
History
DepositionJan 9, 2004Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Mar 2, 2004Provider: repository / Type: Initial release
Revision 1.1Apr 27, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Derived calculations / Version format compliance
Revision 1.3Dec 27, 2023Group: Data collection / Database references / Derived calculations
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_struct_conn_angle / struct_conn / struct_ref_seq_dif / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_asym_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_conn.ptnr2_label_seq_id / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Kinesin-like protein KIF2C
hetero molecules


Theoretical massNumber of molelcules
Total (without water)47,3333
Polymers46,8031
Non-polymers5312
Water2,000111
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPQS
2
A: Kinesin-like protein KIF2C
hetero molecules

A: Kinesin-like protein KIF2C
hetero molecules

A: Kinesin-like protein KIF2C
hetero molecules

A: Kinesin-like protein KIF2C
hetero molecules


Theoretical massNumber of molelcules
Total (without water)189,33312
Polymers187,2114
Non-polymers2,1228
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation2_365-x-2,-y+1,z1
crystal symmetry operation3_355-x-2,y,-z1
crystal symmetry operation4_565x,-y+1,-z1
Buried area13580 Å2
ΔGint-113 kcal/mol
Surface area56000 Å2
MethodPISA
Unit cell
Length a, b, c (Å)61.068, 191.475, 74.627
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number21
Space group name H-MC222

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Components

#1: Protein Kinesin-like protein KIF2C / Mitotic centromere-associated kinesin / MCAK


Mass: 46802.711 Da / Num. of mol.: 1 / Fragment: RESIDUES 1-403
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Gene: KIF2C / Plasmid: pET21b / Production host: Escherichia coli (E. coli) / References: UniProt: Q922S8
#2: Chemical ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Mg
#3: Chemical ChemComp-ANP / PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER


Mass: 506.196 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C10H17N6O12P3 / Comment: AMP-PNP, energy-carrying molecule analogue*YM
#4: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 111 / 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: 2.81 Å3/Da / Density % sol: 55.88 %
Crystal growTemperature: 297 K / Method: vapor diffusion, hanging drop / pH: 6
Details: potassium sodium tartrate tetrahydrate, MES, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 297.0K
Crystal grow
*PLUS
Temperature: 24 ℃ / Method: vapor diffusion, hanging drop
Components of the solutions
*PLUS
IDConc.Common nameCrystal-IDSol-IDDetails
110 mg/mlprotein1drop
21.0 Mpotassium sodium tartrate tetrahydrate1reservoir
30.1 MMES1reservoirpH6.0

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Data collection

DiffractionMean temperature: 95 K
Diffraction sourceSource: SYNCHROTRON / Site: Photon Factory / Beamline: AR-NW12A / Wavelength: 0.98 Å
DetectorType: ADSC QUANTUM 210 / Detector: CCD / Date: Jun 11, 2003
RadiationMonochromator: double flat Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.98 Å / Relative weight: 1
ReflectionResolution: 2.24→47.9 Å / Num. all: 21219 / Num. obs: 20584 / % possible obs: 96.2 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Biso Wilson estimate: 32.2 Å2
Reflection shellResolution: 2.25→2.39 Å / % possible all: 86.6
Reflection
*PLUS
Highest resolution: 2.25 Å / Lowest resolution: 50 Å / % possible obs: 98.5 % / Rmerge(I) obs: 0.086

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Processing

Software
NameVersionClassification
CNS1refinement
HKL-2000data reduction
SCALEPACKdata scaling
CNSphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.25→23.94 Å / Rfactor Rfree error: 0.006 / Data cutoff high absF: 979129.57 / 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
Rfree0.252 2004 9.8 %RANDOM
Rwork0.215 ---
all0.238 ---
obs0.215 20437 96.2 %-
Solvent computationSolvent model: FLAT MODEL / Bsol: 58.4229 Å2 / ksol: 0.379531 e/Å3
Displacement parametersBiso mean: 51.6 Å2
Baniso -1Baniso -2Baniso -3
1--0.84 Å20 Å20 Å2
2---15.81 Å20 Å2
3---16.65 Å2
Refine analyze
FreeObs
Luzzati coordinate error0.33 Å0.27 Å
Luzzati d res low-5 Å
Luzzati sigma a0.33 Å0.26 Å
Refinement stepCycle: LAST / Resolution: 2.25→23.94 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms2630 0 32 111 2773
Refine LS restraints
Refine-IDTypeDev idealDev ideal target
X-RAY DIFFRACTIONc_bond_d0.009
X-RAY DIFFRACTIONc_angle_deg1.7
X-RAY DIFFRACTIONc_dihedral_angle_d24.3
X-RAY DIFFRACTIONc_improper_angle_d1.27
X-RAY DIFFRACTIONc_mcbond_it3.171.5
X-RAY DIFFRACTIONc_mcangle_it4.572
X-RAY DIFFRACTIONc_scbond_it5.242
X-RAY DIFFRACTIONc_scangle_it6.82.5
LS refinement shellResolution: 2.25→2.39 Å / Rfactor Rfree error: 0.017 / Total num. of bins used: 6
RfactorNum. reflection% reflection
Rfree0.292 290 9.7 %
Rwork0.265 2715 -
obs--86.6 %
Xplor file
Refine-IDSerial noParam fileTopol file
X-RAY DIFFRACTION1PROTEIN_REP.PARAMPROTEIN.TOP
X-RAY DIFFRACTION2ANP.PARAMANP.TOP
X-RAY DIFFRACTION3ION.PARAMION.TOP
X-RAY DIFFRACTION4WATER_REP.PARAMWATER_REP.TOP
Refinement
*PLUS
Lowest resolution: 24 Å
Solvent computation
*PLUS
Displacement parameters
*PLUS
Refine LS restraints
*PLUS
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONc_dihedral_angle_d
X-RAY DIFFRACTIONc_dihedral_angle_deg24.3
X-RAY DIFFRACTIONc_improper_angle_d
X-RAY DIFFRACTIONc_improper_angle_deg1.27

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