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Open data
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Basic information
Entry | Database: PDB / ID: 3zyc | ||||||
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Title | DYNAMIN 1 GTPASE GED FUSION DIMER COMPLEXED WITH GMPPCP | ||||||
![]() | DYNAMIN-1 | ||||||
![]() | HYDROLASE / MEMBRANE FISSION / NUCLEOTIDE-BINDING / ENDOCYTOSIS / MOTOR PROTEIN | ||||||
Function / homology | ![]() clathrin coat assembly involved in endocytosis / vesicle scission / synaptic vesicle budding from presynaptic endocytic zone membrane / presynaptic endocytic zone membrane / dynamin GTPase / chromaffin granule / regulation of vesicle size / Toll Like Receptor 4 (TLR4) Cascade / Retrograde neurotrophin signalling / endosome organization ...clathrin coat assembly involved in endocytosis / vesicle scission / synaptic vesicle budding from presynaptic endocytic zone membrane / presynaptic endocytic zone membrane / dynamin GTPase / chromaffin granule / regulation of vesicle size / Toll Like Receptor 4 (TLR4) Cascade / Retrograde neurotrophin signalling / endosome organization / Formation of annular gap junctions / photoreceptor ribbon synapse / Gap junction degradation / membrane coat / Recycling pathway of L1 / phosphatidylinositol-3,4,5-trisphosphate binding / endocytic vesicle / EPH-ephrin mediated repulsion of cells / clathrin-coated pit / phosphatidylinositol-4,5-bisphosphate binding / MHC class II antigen presentation / photoreceptor inner segment / receptor-mediated endocytosis / cell projection / modulation of chemical synaptic transmission / protein homooligomerization / receptor internalization / endocytosis / GDP binding / Clathrin-mediated endocytosis / presynapse / microtubule binding / protein homotetramerization / microtubule / GTPase activity / glutamatergic synapse / synapse / GTP binding / protein kinase binding / protein homodimerization activity / RNA binding / extracellular exosome / identical protein binding / plasma membrane / cytoplasm Similarity search - Function | ||||||
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Method | ![]() ![]() | ||||||
![]() | Chappie, J.S. / Mears, J.A. / Fang, S. / Leonard, M. / Schmid, S.L. / Milligan, R.A. / Hinshaw, J.E. / Dyda, F. | ||||||
![]() | ![]() Title: A pseudoatomic model of the dynamin polymer identifies a hydrolysis-dependent powerstroke. Authors: Joshua S Chappie / Jason A Mears / Shunming Fang / Marilyn Leonard / Sandra L Schmid / Ronald A Milligan / Jenny E Hinshaw / Fred Dyda / ![]() Abstract: The GTPase dynamin catalyzes membrane fission by forming a collar around the necks of clathrin-coated pits, but the specific structural interactions and conformational changes that drive this process ...The GTPase dynamin catalyzes membrane fission by forming a collar around the necks of clathrin-coated pits, but the specific structural interactions and conformational changes that drive this process remain a mystery. We present the GMPPCP-bound structures of the truncated human dynamin 1 helical polymer at 12.2 Å and a fusion protein, GG, linking human dynamin 1's catalytic G domain to its GTPase effector domain (GED) at 2.2 Å. The structures reveal the position and connectivity of dynamin fragments in the assembled structure, showing that G domain dimers only form between tetramers in sequential rungs of the dynamin helix. Using chemical crosslinking, we demonstrate that dynamin tetramers are made of two dimers, in which the G domain of one molecule interacts in trans with the GED of another. Structural comparison of GG(GMPPCP) to the GG transition-state complex identifies a hydrolysis-dependent powerstroke that may play a role in membrane-remodeling events necessary for fission. | ||||||
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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PDBx/mmCIF format | ![]() | 154.1 KB | Display | ![]() |
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PDB format | ![]() | 119.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 1949C ![]() 3zysC ![]() 2x2eS S: Starting model for refinement C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 |
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (-1, 0.0003, -0.0042), Vector: |
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Components
#1: Protein | Mass: 39388.961 Da / Num. of mol.: 2 Fragment: GTPASE DOMAIN, RESIDUES 6-320, GTPASE EFFECTOR DOMAIN, RESIDUES 726-750 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #2: Chemical | #3: Chemical | #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.19 Å3/Da / Density % sol: 43.71 % / Description: NONE |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, sitting drop / pH: 7 Details: GGGMPPCP WAS CRYSTALLIZED BY SITTING DROP VAPOR DIFFUSION IN 0.1M HEPES PH 7.0, 200 MM MGCL2, AND 24-30% PEG 2000 MME USING A DROP SIZE OF 3 MICROL AND RESERVOIR VOLUME OF 65 MICROL. ...Details: GGGMPPCP WAS CRYSTALLIZED BY SITTING DROP VAPOR DIFFUSION IN 0.1M HEPES PH 7.0, 200 MM MGCL2, AND 24-30% PEG 2000 MME USING A DROP SIZE OF 3 MICROL AND RESERVOIR VOLUME OF 65 MICROL. CRYSTALS GREW IN 3-5 DAYS AT 20C. THE ADDITION OF 200 MM LICL, NACL, KCL, OR NH4CL TO THE RESERVOIR SOLUTION DRAMATICALLY IMPROVED THE CRYSTALS. CRYSTALS GROWN IN THE PRESENCE OF KCL SHOWED THE BEST DIFFRACTION. |
-Data collection
Diffraction | Mean temperature: 95 K |
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Diffraction source | Source: ![]() |
Detector | Type: RIGAKU-MSC SATURN 200 / Detector: CCD / Date: Sep 15, 2010 / Details: CONFOCAL |
Radiation | Monochromator: MULTILAYER MIRROR / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.2→30 Å / Num. obs: 34206 / % possible obs: 99 % / Observed criterion σ(I): -3 / Redundancy: 4.27 % / Rmerge(I) obs: 0.08 / Net I/σ(I): 12.23 |
Reflection shell | Resolution: 2.2→2.26 Å / Redundancy: 2.57 % / Rmerge(I) obs: 0.34 / Mean I/σ(I) obs: 2.95 / % possible all: 90.5 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 2X2E Resolution: 2.2→30 Å / Rfactor Rfree error: 0.009 / Data cutoff high absF: 10000 / Data cutoff low absF: 0 / Cross valid method: THROUGHOUT / σ(F): 0
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Solvent computation | Solvent model: FLAT MODEL / Bsol: 18.5092 Å2 / ksol: 0.34 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Refinement step | Cycle: LAST / Resolution: 2.2→30 Å
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Refine LS restraints |
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Xplor file |
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