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Yorodumi- PDB-4rvo: Crystal structure of a Putative Acyl-CoA ligase (BT_0428) from Ba... -
+Open data
-Basic information
Entry | Database: PDB / ID: 4rvo | |||||||||
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Title | Crystal structure of a Putative Acyl-CoA ligase (BT_0428) from Bacteroides thetaiotaomicron VPI-5482 at 2.41 A resolution | |||||||||
Components | Phenylacetate-coenzyme A ligase | |||||||||
Keywords | LIGASE / Acetyl-CoA synthetase-like / Structural Genomics / Joint Center for Structural Genomics / JCSG / Protein Structure Initiative / PSI-BIOLOGY | |||||||||
Function / homology | Function and homology information phenylacetate-CoA ligase / phenylacetate-CoA ligase activity / phenylacetate catabolic process / nucleotide binding / metal ion binding Similarity search - Function | |||||||||
Biological species | Bacteroides thetaiotaomicron VPI-5482 (bacteria) | |||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MAD / Resolution: 2.41 Å | |||||||||
Authors | Joint Center for Structural Genomics (JCSG) | |||||||||
Citation | Journal: To be published Title: Crystal structure of a Putative Acyl-CoA ligase (BT_0428) from Bacteroides thetaiotaomicron VPI-5482 at 2.41 A resolution Authors: Joint Center for Structural Genomics (JCSG) | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 4rvo.cif.gz | 700.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb4rvo.ent.gz | 607 KB | Display | PDB format |
PDBx/mmJSON format | 4rvo.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/rv/4rvo ftp://data.pdbj.org/pub/pdb/validation_reports/rv/4rvo | HTTPS FTP |
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-Related structure data
Related structure data | |
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Similar structure data | |
Other databases |
-Links
-Assembly
Deposited unit |
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2 |
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Unit cell |
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-Components
-Protein , 1 types, 4 molecules ABCD
#1: Protein | Mass: 50203.996 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Bacteroides thetaiotaomicron VPI-5482 (bacteria) Strain: ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482 / Gene: BT_0428 / Plasmid: SpeedET / Production host: Escherichia Coli (E. coli) / Strain (production host): HK100 / References: UniProt: Q8AAN6 |
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-Non-polymers , 10 types, 587 molecules
#2: Chemical | ChemComp-ZN / #3: Chemical | ChemComp-ADP / #4: Chemical | ChemComp-K / #5: Chemical | ChemComp-UNL / Num. of mol.: 4 / Source method: obtained synthetically #6: Chemical | ChemComp-SO4 / #7: Chemical | ChemComp-PG4 / | #8: Chemical | #9: Chemical | #10: Chemical | ChemComp-EDO / #11: Water | ChemComp-HOH / | |
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-Details
Sequence details | THE CONSTRUCT (RESIDUES 1-435) WAS EXPRESSED WITH A PURIFICATION TAG MGSDKIHHHHHHENLYFQG. THE TAG ...THE CONSTRUCT (RESIDUES 1-435) WAS EXPRESSED WITH A PURIFICATI |
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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: 2.38 Å3/Da / Density % sol: 48.34 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, sitting drop / pH: 6.7 Details: 0.200M potassium sulfate, 20.00% polyethylene glycol 3350, No Buffer pH 6.7, 3mM D-fructose, 3mM CoA, NANODROP, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
-Data collection
Diffraction | Mean temperature: 100 K | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Diffraction source | Source: SYNCHROTRON / Site: SSRL / Beamline: BL9-2 / Wavelength: 0.91837,0.97936,0.97925 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Detector | Type: MARMOSAIC 325 mm CCD / Detector: CCD / Date: Mar 11, 2010 / Details: double crystal monochromator | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Radiation | Monochromator: double crystal / Protocol: MAD / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Radiation wavelength |
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Reflection | Resolution: 2.41→46.574 Å / Num. all: 74114 / Num. obs: 74114 / % possible obs: 99 % / Redundancy: 3.5 % / Rsym value: 0.067 / Net I/σ(I): 12.6 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Reflection shell | Diffraction-ID: 1
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-Phasing
Phasing | Method: MAD |
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-Processing
Software |
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Refinement | Method to determine structure: MAD / Resolution: 2.41→46.574 Å / Cor.coef. Fo:Fc: 0.9425 / Cor.coef. Fo:Fc free: 0.9243 / Occupancy max: 1 / Occupancy min: 0.33 / Cross valid method: THROUGHOUT / σ(F): 0 Details: 1.A MET-INHIBITION PROTOCOL WAS USED FOR SELENOMETHIONINE INCORPORATION DURING PROTEIN EXPRESSION. THE OCCUPANCY OF THE SE ATOMS IN THE MSE RESIDUES WAS REDUCED TO 0.75 FOR THE REDUCED ...Details: 1.A MET-INHIBITION PROTOCOL WAS USED FOR SELENOMETHIONINE INCORPORATION DURING PROTEIN EXPRESSION. THE OCCUPANCY OF THE SE ATOMS IN THE MSE RESIDUES WAS REDUCED TO 0.75 FOR THE REDUCED SCATTERING POWER DUE TO PARTIAL S-MET INCORPORATION. 2.PROTEIN ATOM RECORD CONTAINS SUM OF TLS AND RESIDUAL B FACTORS. ANISOU RECORD CONTAINS SUM OF TLS AND RESIDUAL U FACTORS. 3. NCS RESTRAINTS WERE APPLIED USING BUSTER'S LSSR RESTRAINT REPRESENTATION. 4. POTASSIUM (K) AND SULFATE (SO4) FROM THE CRYSTALLIZATION, AND ETHYLENE GLYCOL (EDO) USED AS A CRYOPROTECTANT WERE MODELED INTO THE STRUCTURE. 5. POLYETHYLENE GLYCOL FRAGMENTS (PEG,PG4,AND PGE FROM THE CRYSTALLIZATION WERE MODELED INTO THE STRUCTURE. 6.ADENOSINE-5'-DIPHOSPHATE WAS MODELED INTO THE ACTIVE SITE ON THE FOUR SUBUNITS. UN-EXPLAINED ELECTRON DENSITIES ADJACENT TO THE ADP WERE MODELED AS UNKNOWN LIGANDS (UNL).7. THE REFINEMENT WAS RESTRAINED AGAINST THE MAD PHASES. 8. TLS GROUPS WERE ASSIGNED WITH WITH THE AID OF THE TLS MOTION SERVER. 9.WATERS AND LIGANDS WERE EXCLUDED FROM TLS REFINEMENT.
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Displacement parameters | Biso max: 153.21 Å2 / Biso mean: 56.9627 Å2 / Biso min: 12.98 Å2
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Refine analyze | Luzzati coordinate error obs: 0.364 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.41→46.574 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.41→2.47 Å / Total num. of bins used: 20
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Refinement TLS params. | Method: refined / Refine-ID: X-RAY DIFFRACTION
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Refinement TLS group |
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