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- PDB-5kx5: Crystal structure of tubulin-stathmin-TTL-Compound 11 complex -

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Basic information

Entry
Database: PDB / ID: 5kx5
TitleCrystal structure of tubulin-stathmin-TTL-Compound 11 complex
Components
  • Stathmin-4
  • TTL protein
  • Tubulin alpha chain
  • Tubulin beta chain
KeywordsSTRUCTURAL PROTEIN/INHIBITOR / Tubulin Tubulysin / STRUCTURAL PROTEIN-INHIBITOR complex
Function / homology
Function and homology information


organelle transport along microtubule / axonemal microtubule / forebrain morphogenesis / glial cell differentiation / neuron projection arborization / cerebellar cortex morphogenesis / flagellated sperm motility / dentate gyrus development / tubulin-tyrosine ligase activity / centrosome cycle ...organelle transport along microtubule / axonemal microtubule / forebrain morphogenesis / glial cell differentiation / neuron projection arborization / cerebellar cortex morphogenesis / flagellated sperm motility / dentate gyrus development / tubulin-tyrosine ligase activity / centrosome cycle / microtubule depolymerization / pyramidal neuron differentiation / motor behavior / smoothened signaling pathway / response to L-glutamate / regulation of synapse organization / startle response / locomotory exploration behavior / microtubule polymerization / sperm flagellum / response to tumor necrosis factor / regulation of microtubule polymerization or depolymerization / microtubule-based process / response to mechanical stimulus / condensed chromosome / homeostasis of number of cells within a tissue / tubulin binding / cellular response to calcium ion / adult locomotory behavior / spindle microtubule / intracellular protein transport / synapse organization / neuromuscular junction / visual learning / protein modification process / recycling endosome / cerebral cortex development / structural constituent of cytoskeleton / memory / microtubule cytoskeleton organization / cytoplasmic ribonucleoprotein granule / neuron migration / neuron projection development / growth cone / neuron apoptotic process / gene expression / microtubule / hydrolase activity / neuron projection / protein heterodimerization activity / nucleotide binding / GTPase activity / protein-containing complex binding / GTP binding / Golgi apparatus / metal ion binding / identical protein binding / plasma membrane / cytosol / cytoplasm
Similarity search - Function
Methane Monooxygenase Hydroxylase; Chain G, domain 1 - #30 / Methane Monooxygenase Hydroxylase; Chain G, domain 1 / Rossmann fold - #11480 / Tubulin-tyrosine ligase/Tubulin polyglutamylase / Tubulin-tyrosine ligase family / TTL domain profile. / Helix hairpin bin / Stathmin family / Stathmin, conserved site / Stathmin superfamily ...Methane Monooxygenase Hydroxylase; Chain G, domain 1 - #30 / Methane Monooxygenase Hydroxylase; Chain G, domain 1 / Rossmann fold - #11480 / Tubulin-tyrosine ligase/Tubulin polyglutamylase / Tubulin-tyrosine ligase family / TTL domain profile. / Helix hairpin bin / Stathmin family / Stathmin, conserved site / Stathmin superfamily / Stathmin family / Stathmin family signature 1. / Stathmin family signature 2. / Stathmin-like (SLD) domain profile. / ATP-grasp fold, A domain / Tubulin/FtsZ, C-terminal domain / Tubulin/FtsZ, GTPase domain / ATP-grasp fold, B domain / D-amino Acid Aminotransferase; Chain A, domain 1 / 60s Ribosomal Protein L30; Chain: A; / Tubulin-beta mRNA autoregulation signal. / Alpha tubulin / 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 / Dna Ligase; domain 1 / Tubulin/FtsZ family, GTPase domain / Tubulin/FtsZ family, GTPase domain / Tubulin/FtsZ, GTPase domain / Tubulin/FtsZ, GTPase domain superfamily / Helix non-globular / Special / Helix Hairpins / Rossmann fold / 2-Layer Sandwich / Orthogonal Bundle / 3-Layer(aba) Sandwich / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
Chem-6YK / ADENOSINE-5'-DIPHOSPHATE / GUANOSINE-5'-DIPHOSPHATE / GUANOSINE-5'-TRIPHOSPHATE / Tubulin beta chain / Tubulin alpha chain / Tubulin tyrosine ligase / Stathmin-4
Similarity search - Component
Biological speciesRattus norvegicus (Norway rat)
Gallus gallus (chicken)
Ovis aries (sheep)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.5 Å
AuthorsParris, K.
CitationJournal: ACS Med Chem Lett / Year: 2016
Title: Design, Synthesis, and Cytotoxic Evaluation of Novel Tubulysin Analogues as ADC Payloads.
Authors: Leverett, C.A. / Sukuru, S.C. / Vetelino, B.C. / Musto, S. / Parris, K. / Pandit, J. / Loganzo, F. / Varghese, A.H. / Bai, G. / Liu, B. / Liu, D. / Hudson, S. / Doppalapudi, V.R. / Stock, J. ...Authors: Leverett, C.A. / Sukuru, S.C. / Vetelino, B.C. / Musto, S. / Parris, K. / Pandit, J. / Loganzo, F. / Varghese, A.H. / Bai, G. / Liu, B. / Liu, D. / Hudson, S. / Doppalapudi, V.R. / Stock, J. / O'Donnell, C.J. / Subramanyam, C.
History
DepositionJul 20, 2016Deposition site: RCSB / Processing site: RCSB
Revision 1.0Dec 28, 2016Provider: repository / Type: Initial release
Revision 1.1Oct 4, 2023Group: 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 / pdbx_initial_refinement_model / pdbx_struct_conn_angle / struct_conn
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_asym_id / _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.ptnr2_auth_asym_id / _pdbx_struct_conn_angle.ptnr2_auth_comp_id / _pdbx_struct_conn_angle.ptnr2_auth_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr2_label_atom_id / _pdbx_struct_conn_angle.ptnr2_label_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_asym_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_asym_id / _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_asym_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

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Tubulin alpha chain
B: Tubulin beta chain
C: Tubulin alpha chain
D: Tubulin beta chain
E: Stathmin-4
F: TTL protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)265,69823
Polymers261,5466
Non-polymers4,15217
Water2,180121
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area23640 Å2
ΔGint-163 kcal/mol
Surface area78240 Å2
MethodPISA
Unit cell
Length a, b, c (Å)104.790, 153.900, 185.200
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number19
Space group name H-MP212121

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Components

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Protein , 4 types, 6 molecules ACBDEF

#1: Protein Tubulin alpha chain


Mass: 50188.441 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Ovis aries (sheep) / References: UniProt: D0VWZ0
#2: Protein Tubulin beta chain


Mass: 49969.797 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Ovis aries (sheep) / References: UniProt: D0VWY9
#3: Protein Stathmin-4 / Stathmin-like protein B3 / RB3


Mass: 16851.133 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Rattus norvegicus (Norway rat) / Gene: Stmn4 / Production host: Escherichia coli (E. coli) / References: UniProt: P63043
#4: Protein TTL protein


Mass: 44378.496 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Gallus gallus (chicken) / Gene: TTL / Production host: Escherichia coli (E. coli) / References: UniProt: E1BQ43

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Non-polymers , 7 types, 138 molecules

#5: Chemical ChemComp-GTP / GUANOSINE-5'-TRIPHOSPHATE


Mass: 523.180 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C10H16N5O14P3 / Comment: GTP, energy-carrying molecule*YM
#6: Chemical
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: Mg
#7: Chemical
ChemComp-CA / CALCIUM ION


Mass: 40.078 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Ca
#8: Chemical ChemComp-GDP / GUANOSINE-5'-DIPHOSPHATE


Type: RNA linking / Mass: 443.201 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C10H15N5O11P2 / Comment: GDP, energy-carrying molecule*YM
#9: Chemical ChemComp-6YK / (2~{S},4~{R})-4-[[2-[(1~{R},3~{R})-1-acetyloxy-3-[[(2~{S},3~{S})-2-[[(2~{R})-1,2-dimethylpyrrolidin-2-yl]carbonylamino]-3-methyl-pentanoyl]-methyl-amino]-4-methyl-pentyl]-1,3-thiazol-4-yl]carbonylamino]-5-(4-aminophenyl)-2-methyl-pentanoic acid


Type: peptide-like / Mass: 742.968 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C38H58N6O7S
#10: Chemical ChemComp-ADP / ADENOSINE-5'-DIPHOSPHATE


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


Mass: 18.015 Da / Num. of mol.: 121 / 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: 2.86 Å3/Da / Density % sol: 56.96 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 6.7
Details: precipitant solution: 3% PEG 4K, 4-6% glycerol, 30 mM MgCl2, 30 mM CaCl2, 100 mM MES/Imidazole pH 6.7

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 17-ID / Wavelength: 1 Å
DetectorType: DECTRIS PILATUS3 S 6M / Detector: PIXEL / Date: Oct 30, 2013
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 2.5→38.47 Å / Num. obs: 101681 / % possible obs: 97.8 % / Redundancy: 5.9 % / Biso Wilson estimate: 67.62 Å2 / Rmerge(I) obs: 0.152 / Net I/av σ(I): 8.8 / Net I/σ(I): 3.6
Reflection shell
Resolution (Å)Redundancy (%)Diffraction-ID% possible allRmerge(I) obs
2.5-2.542.6178.4
2.54-2.593.2186.9
2.59-2.643.8193.6
2.64-2.694.3198
2.69-2.754.8199.8
2.75-2.825.21100
2.82-2.896.11100
2.89-2.966.21100
2.96-3.056.811000.864
3.05-3.156.911000.707
3.15-3.266.911000.553
3.26-3.396.811000.424
3.39-3.556.611000.312
3.55-3.736.411000.223
3.73-3.976.511000.159
3.97-4.27711000.123
4.27-4.716.911000.086
4.71-5.396.411000.086
5.39-6.796.611000.095
6.79-1006.3199.60.045

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Processing

Software
NameVersionClassification
SCALEPACKdata scaling
BUSTER-TNT2.11.6refinement
PDB_EXTRACT3.2data extraction
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 4I55

4i55


Resolution: 2.5→38.47 Å / Cor.coef. Fo:Fc: 0.9423 / Cor.coef. Fo:Fc free: 0.9093 / SU R Cruickshank DPI: 0.382 / Cross valid method: THROUGHOUT / σ(F): 0 / SU R Blow DPI: 0.364 / SU Rfree Blow DPI: 0.258 / SU Rfree Cruickshank DPI: 0.265
RfactorNum. reflection% reflectionSelection details
Rfree0.2514 5070 5.02 %RANDOM
Rwork0.1969 ---
obs0.1996 101079 97.19 %-
Displacement parametersBiso max: 186.62 Å2 / Biso mean: 67.57 Å2 / Biso min: 18.98 Å2
Baniso -1Baniso -2Baniso -3
1-0.8247 Å20 Å20 Å2
2---9.072 Å20 Å2
3---8.2473 Å2
Refine analyzeLuzzati coordinate error obs: 0.372 Å
Refinement stepCycle: final / Resolution: 2.5→38.47 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms17363 0 261 121 17745
Biso mean--66.59 52.97 -
Num. residues----2193
Refine LS restraints
Refine-IDTypeNumberRestraint functionWeightDev ideal
X-RAY DIFFRACTIONt_dihedral_angle_d6338SINUSOIDAL2
X-RAY DIFFRACTIONt_trig_c_planes485HARMONIC2
X-RAY DIFFRACTIONt_gen_planes2707HARMONIC5
X-RAY DIFFRACTIONt_it18070HARMONIC20
X-RAY DIFFRACTIONt_nbd1SEMIHARMONIC5
X-RAY DIFFRACTIONt_improper_torsion
X-RAY DIFFRACTIONt_pseud_angle
X-RAY DIFFRACTIONt_chiral_improper_torsion2332SEMIHARMONIC5
X-RAY DIFFRACTIONt_sum_occupancies
X-RAY DIFFRACTIONt_utility_distance
X-RAY DIFFRACTIONt_utility_angle
X-RAY DIFFRACTIONt_utility_torsion
X-RAY DIFFRACTIONt_ideal_dist_contact20359SEMIHARMONIC4
X-RAY DIFFRACTIONt_bond_d18070HARMONIC20.01
X-RAY DIFFRACTIONt_angle_deg24515HARMONIC21.16
X-RAY DIFFRACTIONt_omega_torsion2.92
X-RAY DIFFRACTIONt_other_torsion20.56
LS refinement shellResolution: 2.5→2.56 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.282 279 4.95 %
Rwork0.2419 5352 -
all0.2439 5631 -
obs--74.25 %

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