+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-43482 | |||||||||
---|---|---|---|---|---|---|---|---|---|---|
Title | Density map for gamma tubulin ring complex capped microtubule | |||||||||
Map data | Density map for gamma tubulin ring complex capped microtubule. | |||||||||
Sample |
| |||||||||
Keywords | Microtubule nucleation complex bound to a microtubule / CELL CYCLE | |||||||||
Function / homology | Function and homology information netrin receptor binding / microtubule nucleation by interphase microtubule organizing center / gamma-tubulin complex localization / positive regulation of norepinephrine uptake / cellular response to cytochalasin B / regulation of transepithelial transport / equatorial microtubule organizing center / Post-chaperonin tubulin folding pathway / morphogenesis of a polarized epithelium / dorsal root ganglion development ...netrin receptor binding / microtubule nucleation by interphase microtubule organizing center / gamma-tubulin complex localization / positive regulation of norepinephrine uptake / cellular response to cytochalasin B / regulation of transepithelial transport / equatorial microtubule organizing center / Post-chaperonin tubulin folding pathway / morphogenesis of a polarized epithelium / dorsal root ganglion development / bBAF complex / mitotic spindle microtubule / Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane / gamma-tubulin ring complex / Cilium Assembly / microtubule minus-end binding / interphase microtubule organizing center / postsynaptic actin cytoskeleton organization / Carboxyterminal post-translational modifications of tubulin / protein localization to adherens junction / postsynaptic actin cytoskeleton / polar microtubule / npBAF complex / gamma-tubulin complex / Tat protein binding / brahma complex / structural constituent of postsynaptic actin cytoskeleton / nBAF complex / GBAF complex / meiotic spindle organization / regulation of G0 to G1 transition / dense body / Formation of annular gap junctions / Sealing of the nuclear envelope (NE) by ESCRT-III / Intraflagellar transport / Gap junction degradation / cytoskeleton-dependent intracellular transport / Cell-extracellular matrix interactions / Folding of actin by CCT/TriC / apical protein localization / regulation of double-strand break repair / microtubule nucleation / Formation of tubulin folding intermediates by CCT/TriC / Gap junction assembly / regulation of nucleotide-excision repair / adherens junction assembly / COPI-independent Golgi-to-ER retrograde traffic / Prefoldin mediated transfer of substrate to CCT/TriC / RSC-type complex / RHOF GTPase cycle / gamma-tubulin binding / Adherens junctions interactions / non-motile cilium / tight junction / Assembly and cell surface presentation of NMDA receptors / Kinesins / Sensory processing of sound by outer hair cells of the cochlea / regulation of norepinephrine uptake / regulation of mitotic metaphase/anaphase transition / Interaction between L1 and Ankyrins / Sensory processing of sound by inner hair cells of the cochlea / SWI/SNF complex / positive regulation of double-strand break repair / regulation of synaptic vesicle endocytosis / positive regulation of T cell differentiation / COPI-dependent Golgi-to-ER retrograde traffic / apical junction complex / microtubule organizing center / establishment or maintenance of cell polarity / regulation of cyclin-dependent protein serine/threonine kinase activity / cortical cytoskeleton / maintenance of blood-brain barrier / intercellular bridge / positive regulation of stem cell population maintenance / NuA4 histone acetyltransferase complex / nitric-oxide synthase binding / pericentriolar material / cell leading edge / Recycling pathway of L1 / regulation of G1/S transition of mitotic cell cycle / cytoplasmic microtubule / kinesin binding / mitotic sister chromatid segregation / brush border / microtubule-based process / calyx of Held / negative regulation of cell differentiation / RHOH GTPase cycle / positive regulation of double-strand break repair via homologous recombination / mitotic spindle assembly / EPH-ephrin mediated repulsion of cells / single fertilization / RHO GTPases Activate WASPs and WAVEs / RHO GTPases activate IQGAPs / regulation of protein localization to plasma membrane / spindle assembly / positive regulation of myoblast differentiation / cellular response to interleukin-4 / Hedgehog 'off' state / COPI-mediated anterograde transport Similarity search - Function | |||||||||
Biological species | Homo sapiens (human) | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 7.7 Å | |||||||||
Authors | Aher A / Urnavicius L / Kapoor TM | |||||||||
Funding support | United States, 1 items
| |||||||||
Citation | Journal: Nat Struct Mol Biol / Year: 2024 Title: Structure of the γ-tubulin ring complex-capped microtubule. Authors: Amol Aher / Linas Urnavicius / Allen Xue / Kasahun Neselu / Tarun M Kapoor / Abstract: Microtubules are composed of α-tubulin and β-tubulin dimers positioned head-to-tail to form protofilaments that associate laterally in varying numbers. It is not known how cellular microtubules ...Microtubules are composed of α-tubulin and β-tubulin dimers positioned head-to-tail to form protofilaments that associate laterally in varying numbers. It is not known how cellular microtubules assemble with the canonical 13-protofilament architecture, resulting in micrometer-scale α/β-tubulin tracks for intracellular transport that align with, rather than spiral along, the long axis of the filament. We report that the human ~2.3 MDa γ-tubulin ring complex (γ-TuRC), an essential regulator of microtubule formation that contains 14 γ-tubulins, selectively nucleates 13-protofilament microtubules. Cryogenic electron microscopy reconstructions of γ-TuRC-capped microtubule minus ends reveal the extensive intra-domain and inter-domain motions of γ-TuRC subunits that accommodate luminal bridge components and establish lateral and longitudinal interactions between γ-tubulins and α-tubulins. Our structures suggest that γ-TuRC, an inefficient nucleation template owing to its splayed conformation, can transform into a compacted cap at the microtubule minus end and set the lattice architecture of cellular microtubules. | |||||||||
History |
|
-Structure visualization
Supplemental images |
---|
-Downloads & links
-EMDB archive
Map data | emd_43482.map.gz | 36.3 MB | EMDB map data format | |
---|---|---|---|---|
Header (meta data) | emd-43482-v30.xml emd-43482.xml | 29.7 KB 29.7 KB | Display Display | EMDB header |
FSC (resolution estimation) | emd_43482_fsc.xml | 12.9 KB | Display | FSC data file |
Images | emd_43482.png | 88.5 KB | ||
Filedesc metadata | emd-43482.cif.gz | 10.4 KB | ||
Others | emd_43482_half_map_1.map.gz emd_43482_half_map_2.map.gz | 140.6 MB 140.6 MB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-43482 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-43482 | HTTPS FTP |
-Validation report
Summary document | emd_43482_validation.pdf.gz | 1001.6 KB | Display | EMDB validaton report |
---|---|---|---|---|
Full document | emd_43482_full_validation.pdf.gz | 1001.2 KB | Display | |
Data in XML | emd_43482_validation.xml.gz | 19.9 KB | Display | |
Data in CIF | emd_43482_validation.cif.gz | 26.3 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-43482 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-43482 | HTTPS FTP |
-Related structure data
Related structure data | 8vrjMC 8vrkC 8vt7C M: atomic model generated by this map C: citing same article (ref.) |
---|---|
Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
---|---|
Related items in Molecule of the Month |
-Map
File | Download / File: emd_43482.map.gz / Format: CCP4 / Size: 178 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Annotation | Density map for gamma tubulin ring complex capped microtubule. | ||||||||||||||||||||
Voxel size | X=Y=Z: 1.32 Å | ||||||||||||||||||||
Density |
| ||||||||||||||||||||
Symmetry | Space group: 1 | ||||||||||||||||||||
Details | EMDB XML:
|
-Supplemental data
-Half map: Half map for gamma tubulin ring complex capped microtubule.
File | emd_43482_half_map_1.map | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Annotation | Half map for gamma tubulin ring complex capped microtubule. | ||||||||||||
Projections & Slices |
| ||||||||||||
Density Histograms |
-Half map: Half map for gamma tubulin ring complex capped microtubule.
File | emd_43482_half_map_2.map | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Annotation | Half map for gamma tubulin ring complex capped microtubule. | ||||||||||||
Projections & Slices |
| ||||||||||||
Density Histograms |
-Sample components
+Entire : Gamma tubulin ring complex bound to microtubule minus end
+Supramolecule #1: Gamma tubulin ring complex bound to microtubule minus end
+Macromolecule #1: Tubulin alpha-1B chain
+Macromolecule #2: Tubulin beta-3 chain
+Macromolecule #3: TUBGCP6 protein
+Macromolecule #4: Gamma-tubulin complex component 3
+Macromolecule #5: Mitotic-spindle organizing protein 1
+Macromolecule #6: Actin, cytoplasmic 1
+Macromolecule #7: Isoform 3 of Gamma-tubulin complex component 2
+Macromolecule #8: Isoform 2 of Gamma-tubulin complex component 4
+Macromolecule #9: Gamma-tubulin complex component 5
+Macromolecule #10: Tubulin gamma-1 chain
-Experimental details
-Structure determination
Method | cryo EM |
---|---|
Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Buffer | pH: 6.8 |
---|---|
Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % |
-Electron microscopy
Microscope | FEI TITAN KRIOS |
---|---|
Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 60.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 3.5 µm / Nominal defocus min: 1.5 µm |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |
+Image processing
-Atomic model buiding 1
Refinement | Protocol: RIGID BODY FIT |
---|---|
Output model | PDB-8vrj: |