+Open data
-Basic information
Entry | Database: PDB / ID: 8smm | ||||||||||||
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Title | Xenopus laevis hyaluronan synthase 1 | ||||||||||||
Components |
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Keywords | Transferase/Immune System / hyaluronic acid / hyaluronan / HA / HAS / glycosyltransferase / GT / membrane protein / Fab / Transferase-Immune System complex | ||||||||||||
Function / homology | hyaluronan synthase / Chitin synthase / hyaluronan synthase activity / extracellular matrix assembly / hyaluronan biosynthetic process / extracellular polysaccharide biosynthetic process / Nucleotide-diphospho-sugar transferases / membrane / Hyaluronan synthase 1 Function and homology information | ||||||||||||
Biological species | Xenopus laevis (African clawed frog) Homo sapiens (human) | ||||||||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.2 Å | ||||||||||||
Authors | Gorniak, I. / Zimmer, J. | ||||||||||||
Funding support | United States, Germany, 3items
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Citation | Journal: To Be Published Title: Atomistic insights into hyaluronan synthesis, secretion, and length control Authors: Gorniak, I. / Stephens, Z.S. / Erramilli, S.K. / Gawda, T. / Kossiakoff, A.A. / Zimmer, J. | ||||||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 8smm.cif.gz | 164.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb8smm.ent.gz | 123.8 KB | Display | PDB format |
PDBx/mmJSON format | 8smm.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/sm/8smm ftp://data.pdbj.org/pub/pdb/validation_reports/sm/8smm | HTTPS FTP |
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-Related structure data
Related structure data | 40591MC 8smnC 8smpC M: map data used to model this data C: citing same article (ref.) |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
-Assembly
Deposited unit |
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1 |
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-Components
#1: Protein | Mass: 70385.047 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Xenopus laevis (African clawed frog) / Gene: has1 / Production host: Spodoptera frugiperda (fall armyworm) / References: UniProt: P13563, hyaluronan synthase |
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#2: Antibody | Mass: 24674.379 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Production host: Spodoptera frugiperda (fall armyworm) |
#3: Antibody | Mass: 23258.783 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Production host: Spodoptera frugiperda (fall armyworm) |
-Experimental details
-Experiment
Experiment | Method: ELECTRON MICROSCOPY |
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EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
-Sample preparation
Component | Name: Xenopus laevis hyaluronan synthase 1 in complex with a Fab molecule Type: COMPLEX / Entity ID: all / Source: RECOMBINANT | ||||||||||||||||||||
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Molecular weight | Value: 0.118 MDa / Experimental value: NO | ||||||||||||||||||||
Source (natural) | Organism: Xenopus laevis (African clawed frog) | ||||||||||||||||||||
Source (recombinant) | Organism: Spodoptera frugiperda (fall armyworm) | ||||||||||||||||||||
Buffer solution | pH: 7.8 | ||||||||||||||||||||
Buffer component |
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Specimen | Conc.: 8 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES | ||||||||||||||||||||
Specimen support | Details: Glow discharged in the presence of 1 drop of amylamine Grid material: COPPER / Grid type: C-flat-1.2/1.3 | ||||||||||||||||||||
Vitrification | Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 277 K |
-Electron microscopy imaging
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |
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Microscopy | Model: FEI TITAN KRIOS |
Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
Electron lens | Mode: BRIGHT FIELDBright-field microscopy / Nominal magnification: 81000 X / Nominal defocus max: 20000 nm / Nominal defocus min: 10000 nm / Cs: 2.7 mm / C2 aperture diameter: 100 µm |
Specimen holder | Cryogen: NITROGEN |
Image recording | Electron dose: 50 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) |
-Processing
EM software |
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CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
Particle selection | Num. of particles selected: 6543217 | ||||||||||||||||||||||||
Symmetry | Point symmetry: C1 (asymmetric) | ||||||||||||||||||||||||
3D reconstruction | Resolution: 3.2 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 305106 / Symmetry type: POINT | ||||||||||||||||||||||||
Atomic model building | Protocol: RIGID BODY FIT | ||||||||||||||||||||||||
Refine LS restraints |
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