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Yorodumi- PDB-5gmy: Crystal structure of the Archaeoglobus fulgidus oligosaccharyltra... -
+Open data
-Basic information
Entry | Database: PDB / ID: 5gmy | |||||||||
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Title | Crystal structure of the Archaeoglobus fulgidus oligosaccharyltransferase (O29867_ARCFU) tethered with an acceptor peptide containing the NVT sequon via a disulfide bond | |||||||||
Components |
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Keywords | TRANSFERASE / Oligosaccharyltransferase / N-lineked glycosylation / AglB / Archaeoglobus fulgidus | |||||||||
Function / homology | Function and homology information dolichyl-phosphooligosaccharide-protein glycotransferase / dolichyl-diphosphooligosaccharide-protein glycotransferase activity / protein N-linked glycosylation via asparagine / post-translational protein modification / metal ion binding / plasma membrane Similarity search - Function | |||||||||
Biological species | Archaeoglobus fulgidus DSM 4304 (archaea) synthetic construct (others) | |||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.5 Å | |||||||||
Authors | Matsumoto, S. / Kohda, D. | |||||||||
Funding support | Japan, 1items
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Citation | Journal: Biochemistry / Year: 2017 Title: Tethering an N-Glycosylation Sequon-Containing Peptide Creates a Catalytically Competent Oligosaccharyltransferase Complex Authors: Matsumoto, S. / Taguchi, Y. / Shimada, A. / Igura, M. / Kohda, D. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 5gmy.cif.gz | 429.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb5gmy.ent.gz | 300.9 KB | Display | PDB format |
PDBx/mmJSON format | 5gmy.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 5gmy_validation.pdf.gz | 446.4 KB | Display | wwPDB validaton report |
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Full document | 5gmy_full_validation.pdf.gz | 457.1 KB | Display | |
Data in XML | 5gmy_validation.xml.gz | 30.3 KB | Display | |
Data in CIF | 5gmy_validation.cif.gz | 40.8 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/gm/5gmy ftp://data.pdbj.org/pub/pdb/validation_reports/gm/5gmy | HTTPS FTP |
-Related structure data
Related structure data | 3wakS S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 99159.875 Da / Num. of mol.: 1 / Mutation: G617C Source method: isolated from a genetically manipulated source Source: (gene. exp.) Archaeoglobus fulgidus DSM 4304 (archaea) Strain: DSM 4304 / Gene: AF_0380 / Production host: Escherichia coli (E. coli) References: UniProt: O29867, dolichyl-diphosphooligosaccharide-protein glycotransferase |
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#2: Protein/peptide | Mass: 826.941 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) synthetic construct (others) |
#3: Chemical | ChemComp-MG / |
Has ligand of interest | N |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 3.35 Å3/Da / Density % sol: 63.28 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 6.5 Details: 10 mM MgCl2, 0.1 M Bis-Tris, pH 6.5, 22 % (w/v) PEG 550MME, 5% (v/v) Jeffamine M-600 |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: SYNCHROTRON / Site: SPring-8 / Beamline: BL44XU / Wavelength: 0.9 Å |
Detector | Type: RAYONIX MX300HE / Detector: CCD / Date: Nov 10, 2013 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9 Å / Relative weight: 1 |
Reflection | Resolution: 3.5→49.9 Å / Num. obs: 17649 / % possible obs: 99.8 % / Redundancy: 13.9 % / Biso Wilson estimate: 147.08 Å2 / Rmerge(I) obs: 0.106 / Net I/σ(I): 44.7 |
Reflection shell | Resolution: 3.5→3.56 Å / Redundancy: 14.2 % / Rmerge(I) obs: 1.283 / Mean I/σ(I) obs: 3.6 / Num. unique obs: 828 / CC1/2: 0.956 / % possible all: 100 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 3WAK Resolution: 3.5→40.1 Å / SU ML: 0.5571 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 35.3813 Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 202.48 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 3.5→40.1 Å
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Refine LS restraints |
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LS refinement shell |
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Refinement TLS params. | Method: refined / Refine-ID: X-RAY DIFFRACTION
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Refinement TLS group | Refine-ID: X-RAY DIFFRACTION
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