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Yorodumi- PDB-2ux8: Crystal Structure of Sphingomonas elodea ATCC 31461 Glucose-1- ph... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2ux8 | ||||||
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Title | Crystal Structure of Sphingomonas elodea ATCC 31461 Glucose-1- phosphate uridylyltransferase in Complex with glucose-1-phosphate. | ||||||
Components | GLUCOSE-1-PHOSPHATE URIDYLYLTRANSFERASE | ||||||
Keywords | TRANSFERASE / UGPG / GALU PYROPHOSPHORYLASE / GLUCOSE-1-PHOSPHATE URIDYLYLTRANSFERASE / NUCLEOTIDYLTRANSFERASE | ||||||
Function / homology | Function and homology information UTP-glucose-1-phosphate uridylyltransferase / UTP:glucose-1-phosphate uridylyltransferase activity / UDP-glucose metabolic process / biosynthetic process Similarity search - Function | ||||||
Biological species | SPHINGOMONAS ELODEA (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MIRAS / Resolution: 2.65 Å | ||||||
Authors | Aragao, D. / Fialho, A.M. / Marques, A.R. / Frazao, C. / Sa-Correia, I. / Mitchell, E.P. | ||||||
Citation | Journal: J.Bacteriol. / Year: 2007 Title: The Complex of Sphingomonas Elodea Atcc 31461 Glucose-1-Phosphate Uridylyltransferase with Glucose-1-Phosphate Reveals a Novel Quaternary Structure, Unique Among Nucleoside Diphosphate-Sugar ...Title: The Complex of Sphingomonas Elodea Atcc 31461 Glucose-1-Phosphate Uridylyltransferase with Glucose-1-Phosphate Reveals a Novel Quaternary Structure, Unique Among Nucleoside Diphosphate-Sugar Pyrophosphorylase Members. Authors: Aragao, D. / Fialho, A.M. / Marques, A.R. / Mitchell, E.P. / Sa-Correia, I. / Frazao, C. #1: Journal: Acta Crystallogr.,Sect.F / Year: 2006 Title: Cloning, Expression, Purification, Crystallisation and Preliminary Structure Determination of Glucose- 1-Phosphate Uridylyltransferase (Ugpg) Bound to Glucose-1-Phosphate from Sphingomonas Elodea Atcc31461 Authors: Aragao, D. / Marques, A.R. / Frazao, C. / Enguita, F.J. / Carrondo, M.A. / Fialho, A.M. / Sa-Correia, I. / Mitchell, E.P. | ||||||
History |
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Remark 700 | SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "AA" IN EACH CHAIN ON SHEET RECORDS BELOW ... SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "AA" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 18-STRANDED BARREL THIS IS REPRESENTED BY A 19-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. THE SHEETS PRESENTED AS "BA" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 17-STRANDED BARREL THIS IS REPRESENTED BY A 18-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. THE SHEETS PRESENTED AS "EA" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 8-STRANDED BARREL THIS IS REPRESENTED BY A 9-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. THE SHEETS PRESENTED AS "FA" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 8-STRANDED BARREL THIS IS REPRESENTED BY A 9-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. THE SHEETS PRESENTED AS "GA" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 16-STRANDED BARREL THIS IS REPRESENTED BY A 17-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. |
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2ux8.cif.gz | 412.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2ux8.ent.gz | 345.5 KB | Display | PDB format |
PDBx/mmJSON format | 2ux8.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ux/2ux8 ftp://data.pdbj.org/pub/pdb/validation_reports/ux/2ux8 | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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2 |
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Unit cell |
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-Components
#1: Protein | Mass: 32213.961 Da / Num. of mol.: 8 Source method: isolated from a genetically manipulated source Details: CO-CRYSTALLISED WITH GLUCOSE-1-PHOSPHATE / Source: (gene. exp.) SPHINGOMONAS ELODEA (bacteria) / Plasmid: PUGPG2 BASED ON PWH844 / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21 References: UniProt: Q5FYV5, UTP-glucose-1-phosphate uridylyltransferase #2: Sugar | ChemComp-G1P / #3: Water | ChemComp-HOH / | Sequence details | THIS RECOMBINANT PLASMID CARRIES THE UGPG GENE PRECEDED BY A SEQUENCE CODING FOR SIX HISTIDINE ...THIS RECOMBINAN | |
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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: 2.55 Å3/Da / Density % sol: 51.7 % |
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Crystal grow | pH: 4.6 Details: 0.1M AMMONIUM ACETATE, 0.1M SODIUM CITRATE PH=4.6, 15% PEGMME, 5MM G1P, pH 4.60 |
-Data collection
Diffraction | Mean temperature: 100 K | |||||||||
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: ID29 / Wavelength: 0.97564, 1.13980 | |||||||||
Detector | Type: ADSC CCD / Detector: CCD / Date: Sep 12, 2005 / Details: TOROIDAL MIRROR | |||||||||
Radiation | Monochromator: SI(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | |||||||||
Radiation wavelength |
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Reflection | Resolution: 2.65→102 Å / Num. obs: 85566 / % possible obs: 100 % / Observed criterion σ(I): 2 / Redundancy: 5.7 % / Biso Wilson estimate: 50.3 Å2 / Rmerge(I) obs: 0.1 / Net I/σ(I): 14.1 | |||||||||
Reflection shell | Resolution: 2.65→2.67 Å / Redundancy: 3.7 % / Rmerge(I) obs: 0.65 / Mean I/σ(I) obs: 2 / % possible all: 100 |
-Processing
Software |
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Refinement | Method to determine structure: MIRAS / Resolution: 2.65→74.9 Å / Rfactor Rfree error: 0.007 / Data cutoff high absF: 884457.43 / Isotropic thermal model: B-GROUP / Cross valid method: THROUGHOUT / σ(F): 0 Stereochemistry target values: MAXIMUM LIKELIHOOD TARGET USING AMPLITUDES Details: DIFFERENT NCS RESTRAINS USED FOR MAIN-CHAINS AND FOR SIDE-CHAINS. GROUP B-FACTOR REFINEMENT DOES NOT ALLOW NCS RESTRAINS. DISORDERED REGIONS WERE NOT INCLUDED IN THE REFINEMENT.
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Solvent computation | Solvent model: CNS BULK SOLVENT MODEL USED / Bsol: 45.5985 Å2 / ksol: 0.351613 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 54.23 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.65→74.9 Å
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Refine LS restraints |
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Refine LS restraints NCS | NCS model details: RESTRAINS / Rms dev position: 2 Å / Weight position: 10 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
LS refinement shell | Resolution: 2.75→2.77 Å / Total num. of bins used: 39
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Xplor file | Serial no: 1 / Param file: PROTEIN_REP.PARAM |