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- PDB-7evg: Apo Odinarchaeota tubulin (OdinTubulin) H393D mutant, in a psuedo... -

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Basic information

Entry
Database: PDB / ID: 7evg
TitleApo Odinarchaeota tubulin (OdinTubulin) H393D mutant, in a psuedo-protofilament arrangement
ComponentsTubulin-like protein
KeywordsSTRUCTURAL PROTEIN / Asgard / tubulin / GTP / filament
Function / homology
Function and homology information


microtubule-based process / structural constituent of cytoskeleton / microtubule / GTPase activity / GTP binding
Similarity search - Function
Beta tubulin / Tubulin / Tubulin, C-terminal / Tubulin C-terminal domain / Tubulin, conserved site / Tubulin subunits alpha, beta, and gamma signature. / Tubulin/FtsZ, C-terminal / Tubulin/FtsZ, 2-layer sandwich domain / Tubulin/FtsZ family, GTPase domain / Tubulin/FtsZ family, GTPase domain ...Beta tubulin / Tubulin / Tubulin, C-terminal / Tubulin C-terminal domain / Tubulin, conserved site / Tubulin subunits alpha, beta, and gamma signature. / 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
Similarity search - Domain/homology
PHOSPHATE ION / Tubulin-like protein CetZ
Similarity search - Component
Biological speciesOdinarchaeota archaeon
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.48 Å
AuthorsRobinson, R.C. / Akil, C. / Tran, L.T.
Funding support Japan, United States, 4items
OrganizationGrant numberCountry
Japan Science and TechnologyJPMJCR19S5 Japan
Japan Society for the Promotion of Science (JSPS)JP20H00476 Japan
Simons FoundationGBMF9743 United States
Other privateMoore Foundation GBMF9743 United States
CitationJournal: Sci Adv / Year: 2022
Title: Structure and dynamics of Odinarchaeota tubulin and the implications for eukaryotic microtubule evolution.
Authors: Caner Akıl / Samson Ali / Linh T Tran / Jérémie Gaillard / Wenfei Li / Kenichi Hayashida / Mika Hirose / Takayuki Kato / Atsunori Oshima / Kosuke Fujishima / Laurent Blanchoin / Akihiro ...Authors: Caner Akıl / Samson Ali / Linh T Tran / Jérémie Gaillard / Wenfei Li / Kenichi Hayashida / Mika Hirose / Takayuki Kato / Atsunori Oshima / Kosuke Fujishima / Laurent Blanchoin / Akihiro Narita / Robert C Robinson /
Abstract: Tubulins are critical for the internal organization of eukaryotic cells, and understanding their emergence is an important question in eukaryogenesis. Asgard archaea are the closest known prokaryotic ...Tubulins are critical for the internal organization of eukaryotic cells, and understanding their emergence is an important question in eukaryogenesis. Asgard archaea are the closest known prokaryotic relatives to eukaryotes. Here, we elucidated the apo and nucleotide-bound x-ray structures of an Asgard tubulin from hydrothermal living Odinarchaeota (OdinTubulin). The guanosine 5'-triphosphate (GTP)-bound structure resembles a microtubule protofilament, with GTP bound between subunits, coordinating the "+" end subunit through a network of water molecules and unexpectedly by two cations. A water molecule is located suitable for GTP hydrolysis. Time course crystallography and electron microscopy revealed conformational changes on GTP hydrolysis. OdinTubulin forms tubules at high temperatures, with short curved protofilaments coiling around the tubule circumference, more similar to FtsZ, rather than running parallel to its length, as in microtubules. Thus, OdinTubulin represents an evolutionary stage intermediate between prokaryotic FtsZ and eukaryotic microtubule-forming tubulins.
History
DepositionMay 21, 2021Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Mar 23, 2022Provider: repository / Type: Initial release
Revision 1.1Jun 15, 2022Group: Database references / Category: citation / citation_author
Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title
Revision 1.2Nov 29, 2023Group: Data collection / Refinement description
Category: chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model

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Structure visualization

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Assembly

Deposited unit
A: Tubulin-like protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)47,7852
Polymers47,6901
Non-polymers951
Water72140
1


  • Idetical with deposited unit
  • defined by author
  • Evidence: gel filtration
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area230 Å2
ΔGint-7 kcal/mol
Surface area17070 Å2
Unit cell
Length a, b, c (Å)40.102, 94.184, 100.755
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number19
Space group name H-MP212121
Space group name HallP2ac2ab
Symmetry operation#1: x,y,z
#2: x+1/2,-y+1/2,-z
#3: -x,y+1/2,-z+1/2
#4: -x+1/2,-y,z+1/2

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Components

#1: Protein Tubulin-like protein


Mass: 47690.457 Da / Num. of mol.: 1 / Mutation: H393D
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Odinarchaeota archaeon (strain LCB_4) (archaea)
Strain: LCB_4 / Gene: cetZ, OdinLCB4_01330 / Production host: Escherichia coli (E. coli) / References: UniProt: A0A1Q9N9N5
#2: Chemical ChemComp-PO4 / PHOSPHATE ION


Mass: 94.971 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: PO4
#3: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 40 / Source method: isolated from a natural source / Formula: H2O
Has ligand of interestN

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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: 1.99 Å3/Da / Density % sol: 38.34 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop
Details: 25% PEG 1500, 0.1 M SPG, pH 7.0, soaked with 100 mM phosphate for 2 h

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: SPring-8 / Beamline: BL41XU / Wavelength: 1 Å
DetectorType: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Feb 10, 2021
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 2.48→47.1 Å / Num. obs: 14154 / % possible obs: 99.7 % / Redundancy: 6.6 % / Rmerge(I) obs: 0.185 / Rpim(I) all: 0.078 / Rrim(I) all: 0.201 / Net I/σ(I): 8.6
Reflection shellResolution: 2.48→2.57 Å / Rmerge(I) obs: 1.23 / Mean I/σ(I) obs: 1.7 / Num. unique obs: 1525 / CC1/2: 0.576 / Rpim(I) all: 0.516 / Rrim(I) all: 1.34

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Processing

Software
NameVersionClassification
PHENIXv1.17.1refinement
XDSdata reduction
Aimlessdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 6o2r

6o2r


Resolution: 2.48→44.4 Å / Cross valid method: FREE R-VALUE
Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
RfactorNum. reflection% reflection
Rfree0.257 701 -
Rwork0.211 --
obs-14104 99.8 %
Displacement parametersBiso mean: 49.38 Å2
Refinement stepCycle: LAST / Resolution: 2.48→44.4 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms3353 0 5 40 3398
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00233448
X-RAY DIFFRACTIONf_angle_d0.53234674
X-RAY DIFFRACTIONf_chiral_restr0.0426532
X-RAY DIFFRACTIONf_plane_restr0.0037602
X-RAY DIFFRACTIONf_dihedral_angle_d20.11421278
LS refinement shellResolution: 2.48→2.57 Å /
RfactorNum. reflection
Rfree0.3 71
Rwork0.281 1363

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