|Entry||Database: EMDB / ID: EMD-0615|
Tubulin alpha-1B chain / Tubulin beta chain / (ligand) x 3
|Function / homology|
Function and homology information
cytoplasmic microtubule / cellular response to interleukin-4 / microtubule-based process / structural constituent of cytoskeleton / microtubule cytoskeleton organization / neuron migration / double-stranded RNA binding / mitotic cell cycle / microtubule / GTPase activity ...cytoplasmic microtubule / cellular response to interleukin-4 / microtubule-based process / structural constituent of cytoskeleton / microtubule cytoskeleton organization / neuron migration / double-stranded RNA binding / mitotic cell cycle / microtubule / GTPase activity / GTP binding / ubiquitin protein ligase binding / cytoplasm
Tubulin / Beta tubulin / Tubulin/FtsZ, C-terminal domain superfamily / Tubulin/FtsZ, GTPase domain superfamily / Tubulin, C-terminal / Tubulin/FtsZ, 2-layer sandwich domain / Tubulin, conserved site / Beta tubulin, autoregulation binding site / Tubulin/FtsZ, C-terminal / Tubulin/FtsZ, GTPase domain / Alpha tubulin
Tubulin beta chain / Tubulin alpha-1B chain
|Biological species||Pig (pig)|
|Method||helical reconstruction / cryo EM / Resolution: 4.1 Å|
|Authors||Eshun-Wilson L / Zhang R / Portran D / Nachury MV / Toso D / Lohr T / Vendruscolo M / Bonomi M / Fraser JS / Nogales E|
|Funding support|| United States, 1 items |
|Citation||Journal: Proc. Natl. Acad. Sci. U.S.A. / Year: 2019|
Title: Effects of α-tubulin acetylation on microtubule structure and stability.
Authors: Lisa Eshun-Wilson / Rui Zhang / Didier Portran / Maxence V Nachury / Daniel B Toso / Thomas Löhr / Michele Vendruscolo / Massimiliano Bonomi / James S Fraser / Eva Nogales /
Abstract: Acetylation of K40 in α-tubulin is the sole posttranslational modification to mark the luminal surface of microtubules. It is still controversial whether its relationship with microtubule ...Acetylation of K40 in α-tubulin is the sole posttranslational modification to mark the luminal surface of microtubules. It is still controversial whether its relationship with microtubule stabilization is correlative or causative. We have obtained high-resolution cryo-electron microscopy (cryo-EM) reconstructions of pure samples of αTAT1-acetylated and SIRT2-deacetylated microtubules to visualize the structural consequences of this modification and reveal its potential for influencing the larger assembly properties of microtubules. We modeled the conformational ensembles of the unmodified and acetylated states by using the experimental cryo-EM density as a structural restraint in molecular dynamics simulations. We found that acetylation alters the conformational landscape of the flexible loop that contains αK40. Modification of αK40 reduces the disorder of the loop and restricts the states that it samples. We propose that the change in conformational sampling that we describe, at a location very close to the lateral contacts site, is likely to affect microtubule stability and function.
|Validation Report||PDB-ID: 6o2t|
SummaryFull reportAbout validation report
|Structure viewer||EM map: |
Downloads & links
|File||Download / File: emd_0615.map.gz / Format: CCP4 / Size: 515 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)|
|Projections & slices|
Images are generated by Spider.
|Voxel size||X=Y=Z: 1.07 Å|
|Symmetry||Space group: 1|
CCP4 map header:
+Entire Acetylated Microtubule
|Entire||Name: Acetylated Microtubule / Number of components: 6|
+Component #1: cellular-component, Acetylated Microtubule
|Cellular-component||Name: Acetylated Microtubule / Recombinant expression: No|
+Component #2: protein, Tubulin alpha-1B chain
|Protein||Name: Tubulin alpha-1B chain / Number of Copies: 52 / Recombinant expression: No|
|Mass||Theoretical: 50.204445 kDa|
|Source||Species: Pig (pig)|
|Source (natural)||Organ or tissue: Brain|
+Component #3: protein, Tubulin beta chain
|Protein||Name: Tubulin beta chain / Number of Copies: 52 / Recombinant expression: No|
|Mass||Theoretical: 49.90777 kDa|
|Source||Species: Pig (pig)|
|Source (natural)||Organ or tissue: Brain|
+Component #4: ligand, GUANOSINE-5'-TRIPHOSPHATE
|Ligand||Name: GUANOSINE-5'-TRIPHOSPHATEGuanosine triphosphate / Number of Copies: 52 / Recombinant expression: No|
|Mass||Theoretical: 0.52318 kDa|
+Component #5: ligand, MAGNESIUM ION
|Ligand||Name: MAGNESIUM ION / Number of Copies: 52 / Recombinant expression: No|
|Mass||Theoretical: 2.430505 MDa|
+Component #6: ligand, GUANOSINE-5'-DIPHOSPHATE
|Ligand||Name: GUANOSINE-5'-DIPHOSPHATE / Number of Copies: 52 / Recombinant expression: No|
|Mass||Theoretical: 0.443201 kDa|
|Specimen||Specimen state: helical array / Method: cryo EM|
|Helical parameters||Axial symmetry: C1 (asymmetric) / Delta z: 9.3 Å / Delta phi: -27.7 %deg;|
|Sample solution||Specimen conc.: 10 mg/mL|
Buffer solution: Contains 80 mM PIPES, 1 mM MgCl2, 1 mM EGTA, pH 6.8 with KOH (stored at 4 degrees Celsius).
|Vitrification||Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Temperature: 310.15 K / Humidity: 100 % / Details: Blotted for 4 seconds at blot force 10..|
-Electron microscopy imaging
Model: Titan Krios / Image courtesy: FEI Company
|Imaging||Microscope: FEI TITAN KRIOS|
Details: Preliminary grid screening was performed manually and all of the alignments were initially done using a gold calibration grid.
|Electron gun||Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Electron dose: 25 e/Å2 / Illumination mode: FLOOD BEAM|
|Lens||Magnification: 22500.0 X (nominal), 23364.0 X (calibrated) / Cs: 2.7 mm / Imaging mode: BRIGHT FIELD / Defocus: 1500.0 - 2500.0 nm / Energy filter: GIF Quantum LS|
|Specimen Holder||Model: FEI TITAN KRIOS AUTOGRID HOLDER / Temperature: (77.0 - 77.0 K)|
|Camera||Detector: GATAN K2 SUMMIT (4k x 4k)|
|Image acquisition||Number of digital images: 287|
|Processing||Method: helical reconstruction|
|3D reconstruction||Algorithm: FOURIER SPACE / Software: FREALIGN / CTF correction: CTFFIND4 / Resolution: 4.1 Å / Resolution method: FSC 0.143 CUT-OFF|
|FSC plot (resolution estimation)|
-Atomic model buiding
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