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- PDB-5nr4: Crystal structure of Clasp2 TOG1 domain -

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Basic information

Entry
Database: PDB / ID: 5nr4
TitleCrystal structure of Clasp2 TOG1 domain
ComponentsCLIP-associating protein 2
KeywordsSTRUCTURAL PROTEIN / Microtubules / TOG domain / Tubulin
Function / homology
Function and homology information


presynaptic cytoskeleton organization / cortical microtubule plus-end / negative regulation of wound healing, spreading of epidermal cells / positive regulation of basement membrane assembly involved in embryonic body morphogenesis / vesicle targeting / regulation of gastrulation / microtubule anchoring / microtubule organizing center organization / basal cortex / positive regulation of extracellular matrix disassembly ...presynaptic cytoskeleton organization / cortical microtubule plus-end / negative regulation of wound healing, spreading of epidermal cells / positive regulation of basement membrane assembly involved in embryonic body morphogenesis / vesicle targeting / regulation of gastrulation / microtubule anchoring / microtubule organizing center organization / basal cortex / positive regulation of extracellular matrix disassembly / establishment of mitotic spindle localization / kinetochore microtubule / Role of ABL in ROBO-SLIT signaling / regulation of epithelial to mesenchymal transition / dystroglycan binding / negative regulation of focal adhesion assembly / negative regulation of microtubule depolymerization / microtubule nucleation / microtubule plus-end binding / regulation of microtubule-based process / microtubule organizing center / negative regulation of stress fiber assembly / exit from mitosis / regulation of axon extension / establishment or maintenance of cell polarity / positive regulation of epithelial cell migration / cytoplasmic microtubule / Golgi organization / cell leading edge / regulation of microtubule polymerization / platelet-derived growth factor receptor-beta signaling pathway / positive regulation of exocytosis / mitotic spindle assembly / regulation of microtubule polymerization or depolymerization / axonal growth cone / Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal / Mitotic Prometaphase / EML4 and NUDC in mitotic spindle formation / Resolution of Sister Chromatid Cohesion / protein tyrosine kinase binding / mitotic spindle organization / protein localization to plasma membrane / spindle microtubule / regulation of actin cytoskeleton organization / RHO GTPases Activate Formins / trans-Golgi network / kinetochore / ruffle membrane / microtubule cytoskeleton organization / Separation of Sister Chromatids / actin filament binding / cell cortex / microtubule binding / microtubule / cell division / centrosome / glutamatergic synapse / Golgi apparatus / membrane / plasma membrane / cytosol / cytoplasm
Similarity search - Function
CLASP N-terminal domain / CLASP N terminal / Centrosomal protein CEP104-like, TOG domain / TOG domain / TOG / Armadillo-like helical / Armadillo-type fold
Similarity search - Domain/homology
CLIP-associating protein 2
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / SAD / Resolution: 1.198 Å
AuthorsSharma, A. / Olieric, N. / Weinert, T. / Olieric, V. / Steinmetz, M.O.
CitationJournal: Dev. Cell / Year: 2018
Title: CLASP Suppresses Microtubule Catastrophes through a Single TOG Domain.
Authors: Aher, A. / Kok, M. / Sharma, A. / Rai, A. / Olieric, N. / Rodriguez-Garcia, R. / Katrukha, E.A. / Weinert, T. / Olieric, V. / Kapitein, L.C. / Steinmetz, M.O. / Dogterom, M. / Akhmanova, A.
History
DepositionApr 21, 2017Deposition site: PDBE / Processing site: PDBE
Revision 1.0May 30, 2018Provider: repository / Type: Initial release
Revision 1.1Jul 4, 2018Group: Data collection / Database references / Category: citation / citation_author
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year
Revision 1.2Jul 18, 2018Group: Data collection / Database references / Category: citation
Item: _citation.journal_volume / _citation.page_first / _citation.page_last
Revision 1.3Oct 16, 2019Group: Data collection / Category: reflns_shell
Revision 1.4May 8, 2024Group: Data collection / Database references / Category: chem_comp_atom / chem_comp_bond / database_2
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: CLIP-associating protein 2
B: CLIP-associating protein 2


Theoretical massNumber of molelcules
Total (without water)51,5082
Polymers51,5082
Non-polymers00
Water13,872770
1
A: CLIP-associating protein 2


Theoretical massNumber of molelcules
Total (without water)25,7541
Polymers25,7541
Non-polymers00
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
2
B: CLIP-associating protein 2


Theoretical massNumber of molelcules
Total (without water)25,7541
Polymers25,7541
Non-polymers00
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
Unit cell
Length a, b, c (Å)66.083, 47.116, 74.152
Angle α, β, γ (deg.)90.00, 115.83, 90.00
Int Tables number4
Space group name H-MP1211

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Components

#1: Protein CLIP-associating protein 2 / Cytoplasmic linker-associated protein 2 / Protein Orbit homolog 2 / hOrbit2


Mass: 25754.064 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: CLASP2, KIAA0627 / Production host: Escherichia coli (E. coli) / References: UniProt: O75122
#2: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 770 / 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: 2.02 Å3/Da / Density % sol: 39.03 %
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop / pH: 8.5
Details: 30mM Sodium fluoride; 30mM Sodium bromide; 30mM Sodium iodide; 100mM Tris(Base)/Bicine pH 8.5; 12.5% v/v MPD; 12.5% PEG1000; 12.5% PEG3350

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X06DA / Wavelength: 1 Å
DetectorType: DECTRIS PILATUS 2M-F / Detector: PIXEL / Date: Nov 26, 2014
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 1.19→38.5 Å / Num. obs: 128081 / % possible obs: 99 % / Redundancy: 6.2 % / Net I/σ(I): 13.42

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Processing

Software
NameVersionClassification
PHENIX(dev_2420: ???)refinement
XDSdata reduction
XSCALEdata scaling
SHELXCDphasing
RefinementMethod to determine structure: SAD / Resolution: 1.198→38.491 Å / SU ML: 0.13 / Cross valid method: FREE R-VALUE / σ(F): 1.37 / Phase error: 22.21
RfactorNum. reflection% reflection
Rfree0.2136 2003 1.57 %
Rwork0.2003 --
obs0.2005 127811 98.97 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Refinement stepCycle: LAST / Resolution: 1.198→38.491 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms3360 0 0 770 4130
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0083423
X-RAY DIFFRACTIONf_angle_d1.2734612
X-RAY DIFFRACTIONf_dihedral_angle_d14.9691294
X-RAY DIFFRACTIONf_chiral_restr0.079529
X-RAY DIFFRACTIONf_plane_restr0.006584
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
1.1976-1.22750.2971300.29548062X-RAY DIFFRACTION89
1.2275-1.26070.29861330.27988831X-RAY DIFFRACTION98
1.2607-1.29780.25131450.25948968X-RAY DIFFRACTION99
1.2978-1.33970.26651480.2499030X-RAY DIFFRACTION100
1.3397-1.38760.24521420.23759068X-RAY DIFFRACTION100
1.3876-1.44310.23081420.23129003X-RAY DIFFRACTION100
1.4431-1.50880.22491440.21519045X-RAY DIFFRACTION100
1.5088-1.58840.21551440.19979052X-RAY DIFFRACTION100
1.5884-1.68790.21921470.19659118X-RAY DIFFRACTION100
1.6879-1.81820.21161400.19329037X-RAY DIFFRACTION100
1.8182-2.00120.20721520.19489068X-RAY DIFFRACTION100
2.0012-2.29070.19871410.18399098X-RAY DIFFRACTION100
2.2907-2.88590.21411460.19529155X-RAY DIFFRACTION100
2.8859-38.51130.19641490.18539273X-RAY DIFFRACTION100
Refinement TLS params.

Method: refined / Refine-ID: X-RAY DIFFRACTION

IDL112)L122)L132)L222)L232)L332)S11 (Å °)S12 (Å °)S13 (Å °)S21 (Å °)S22 (Å °)S23 (Å °)S31 (Å °)S32 (Å °)S33 (Å °)T112)T122)T132)T222)T232)T332)Origin x (Å)Origin y (Å)Origin z (Å)
13.80772.0297-0.16855.0254-0.43352.3724-0.1037-0.2050.06180.2573-0.18120.0252-0.14890.08360.15890.2984-0.02010.05130.2526-0.00730.221821.0911-7.823951.4476
21.43570.4454-0.01323.8238-0.70521.6157-0.0209-0.1661-0.22110.347-0.1008-0.10110.01530.26180.05670.3115-0.0092-0.00250.23470.01170.170828.6204-12.366848.9594
33.898-2.85161.12532.0893-0.81980.3256-0.0474-0.3937-0.27350.36490.24710.12360.17190.0829-0.0610.415300.09550.35230.05130.369613.94-18.680246.7393
44.3961.7306-0.52251.7974-0.30310.9445-0.00260.07580.06780.00920.02930.0513-0.1853-0.0115-0.02110.1194-0.00450.00010.1416-0.00590.131321.8936-7.052741.2939
51.6080.6868-0.19961.4114-0.18120.95220.0273-0.1008-0.10490.0934-0.07010.04010.053-0.00450.04370.1078-0.00260.00910.1127-0.00350.12624.8309-12.3735.4816
62.82071.66030.42081.93230.40640.77010.0050.0372-0.24680.0475-0.0222-0.19290.11610.04740.0370.09220.00820.00650.11040.00140.144331.5747-14.361129.559
71.23870.9484-0.32111.4995-0.46870.5587-0.02610.06330.116-0.00330.02740.261-0.0153-0.1880.00560.11560.00520.00930.143-0.01110.138222.3433-9.258421.4091
80.4350.4724-0.05052.4970.22020.4340.03240.0118-0.10120.0841-0.0588-0.07860.11950.05370.03430.11340.00880.00650.09890.00260.120931.87-12.861319.6452
94.4212-5.09410.5777.7103-3.30093.85160.00180.139-0.1336-0.15260.06970.28010.2075-0.1639-0.01350.18930.00120.00590.22550.03110.22920.7351-21.100113.7723
100.21820.02840.23311.08730.35920.6526-0.03530.0101-0.0570.02310.0278-0.02640.03930.04720.01030.09670.0130.00960.11160.00410.090731.5501-10.463610.2615
110.4852-0.28530.00991.8047-0.32630.6407-0.00040.0002-0.1088-0.0274-0.0199-0.04130.07880.03520.01730.1296-0.00170.01570.10890.00240.106232.0337-12.52540.0673
120.32150.08810.26980.03570.03390.57380.2366-0.54-0.08870.1942-0.11160.06440.1619-0.340.23070.3702-0.341-0.04470.6983-0.08660.10540.86515.760658.7463
130.66720.37650.16960.8410.08220.540.3375-0.5034-0.27110.2426-0.3088-0.06640.1766-0.0878-0.0070.1848-0.0926-0.03040.28220.01460.155340.110512.173445.3552
140.60480.05750.19410.63080.04131.169-0.0069-0.02480.0203-0.0026-0.0462-0.0218-0.05240.07750.05370.0980.0049-0.0080.10.00610.101239.848314.933427.7737
151.0851-0.2951-0.04721.8514-0.15790.94-0.0688-0.0915-0.0574-0.0635-0.0444-0.15420.18090.26530.10170.16570.05150.02750.17310.02520.109141.122213.282311.4693
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resid 5 through 18 )
2X-RAY DIFFRACTION2chain 'A' and (resid 19 through 33 )
3X-RAY DIFFRACTION3chain 'A' and (resid 34 through 45 )
4X-RAY DIFFRACTION4chain 'A' and (resid 46 through 64 )
5X-RAY DIFFRACTION5chain 'A' and (resid 65 through 102 )
6X-RAY DIFFRACTION6chain 'A' and (resid 103 through 122 )
7X-RAY DIFFRACTION7chain 'A' and (resid 123 through 141 )
8X-RAY DIFFRACTION8chain 'A' and (resid 142 through 159 )
9X-RAY DIFFRACTION9chain 'A' and (resid 160 through 165 )
10X-RAY DIFFRACTION10chain 'A' and (resid 166 through 199 )
11X-RAY DIFFRACTION11chain 'A' and (resid 200 through 229 )
12X-RAY DIFFRACTION12chain 'B' and (resid 10 through 64 )
13X-RAY DIFFRACTION13chain 'B' and (resid 65 through 122 )
14X-RAY DIFFRACTION14chain 'B' and (resid 123 through 199 )
15X-RAY DIFFRACTION15chain 'B' and (resid 200 through 229 )

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