+Open data
-Basic information
Entry | Database: PDB / ID: 1ef0 | ||||||
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Title | CRYSTAL STRUCTURE OF PI-SCEI MINIPRECURSOR | ||||||
Components | PI-SCEI ENDONUCLEASE | ||||||
Keywords | HYDROLASE / endonuclease / protein splicing / mini-precursor | ||||||
Function / homology | Function and homology information Insulin receptor recycling / Transferrin endocytosis and recycling / ROS and RNS production in phagocytes / Amino acids regulate mTORC1 / Golgi lumen acidification / vacuolar proton-transporting V-type ATPase, V1 domain / endosomal lumen acidification / proton-transporting V-type ATPase complex / vacuolar proton-transporting V-type ATPase complex / vacuolar acidification ...Insulin receptor recycling / Transferrin endocytosis and recycling / ROS and RNS production in phagocytes / Amino acids regulate mTORC1 / Golgi lumen acidification / vacuolar proton-transporting V-type ATPase, V1 domain / endosomal lumen acidification / proton-transporting V-type ATPase complex / vacuolar proton-transporting V-type ATPase complex / vacuolar acidification / intron homing / protein metabolic process / intein-mediated protein splicing / fungal-type vacuole membrane / H+-transporting two-sector ATPase / proton-transporting ATPase activity, rotational mechanism / proton transmembrane transport / proton-transporting ATP synthase activity, rotational mechanism / endonuclease activity / Hydrolases; Acting on ester bonds / Golgi membrane / mRNA binding / DNA binding / ATP binding Similarity search - Function | ||||||
Biological species | Saccharomyces cerevisiae (brewer's yeast) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / Resolution: 2.1 Å | ||||||
Authors | Poland, B.W. / Xu, M.-Q. / Quiocho, F.A. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 2000 Title: Structural insights into the protein splicing mechanism of PI-SceI. Authors: Poland, B.W. / Xu, M.Q. / Quiocho, F.A. #1: Journal: Cell(Cambridge,Mass.) / Year: 1997 Title: Crystal Structure of PI-SceI, a Homing Endonuclease with Protein Splicing Activity Authors: Duan, X. / Gimble, F.S. / Quiocho, F.A. #2: Journal: Science / Year: 1990 Title: Protein Splicing Converts the Yeast TFP1 Gene Product to the 69-kD Subunit of the Vacuolar H+-Adenosine Triphosphatase Authors: Kane, P.M. / Yamashiro, C.T. / Wolczyk, D.F. / Neff, N. / Goebl, M. / Stevens, T.H. #3: Journal: Chem.Soc.Rev. / Year: 1998 Title: The chemical basis of protein splicing. Authors: Paulus, H. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1ef0.cif.gz | 179.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1ef0.ent.gz | 142.2 KB | Display | PDB format |
PDBx/mmJSON format | 1ef0.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ef/1ef0 ftp://data.pdbj.org/pub/pdb/validation_reports/ef/1ef0 | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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Unit cell |
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-Components
#1: Protein | Mass: 51803.812 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Details: FROM THE VACUOLAR ATPASE SUBUNIT Source: (gene. exp.) Saccharomyces cerevisiae (brewer's yeast) Plasmid: PVMA29 / Production host: Escherichia coli (E. coli) References: GenBank: 172907, UniProt: P17255*PLUS, EC: 3.6.1.34 #2: Chemical | #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.51 Å3/Da / Density % sol: 50.93 % | ||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 8.5 Details: PEG 3350, Cadmium chloride, magnesium chloride, mercaptoethanol, tric-HCl, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K | ||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Details: drop consists of equal volume of protein and reservoir solutions | ||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: NSLS / Beamline: X4A / Wavelength: 0.9791 |
Detector | Type: RIGAKU RAXIS / Detector: IMAGE PLATE / Date: Oct 1, 1998 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9791 Å / Relative weight: 1 |
Reflection | Resolution: 2.1→20 Å / Num. all: 61089 / Num. obs: 56914 / % possible obs: 93.3 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 2 / Redundancy: 6.8 % / Rmerge(I) obs: 0.101 / Net I/σ(I): 8.6 |
Reflection shell | Resolution: 2.1→20 Å / Redundancy: 6.8 % / Rmerge(I) obs: 0.101 / Num. unique all: 61089 / % possible all: 93.3 |
Reflection | *PLUS Num. obs: 61089 / Num. measured all: 419279 |
Reflection shell | *PLUS % possible obs: 93.3 % |
-Processing
Software |
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Refinement | Resolution: 2.1→20 Å / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 2.1→20 Å
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Refine LS restraints |
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Software | *PLUS Name: 'CNS' / Classification: refinement | |||||||||||||||||||||||||
Refine LS restraints | *PLUS
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